Department of Chemistry course timetable
April 2015
| Fri 17 |
CATALYSIS (CA) (CA2) Metal Catalysis in Evolved Systems (3L) How to handle dioxygen without oxidising yourself. PLEASE NOTE THAT LECTURE 2 ON 15 APRIL HAS BEEN CANCELLED Lecture 1 – Strategies for generating iron oxy species for CH bond oxidation This lecture will look at how mononuclear and dinuclear iron sites can generate iron superoxy, peroxy and oxo species for insertion of O into CH bonds and related activities. It will include a comparison of the activity of the best of synthetic catalysts with what is known about the hugely abundant natural ones. Lecture 2 – The Cytochrome P450 paradigm Cytochromes P450 are a special case of monooxygenases that are widespread across biological systems, and especially important to pharmaceutical companies as modifiers of drugs. The protein engineering of P450s will be discussed. Lecture 3 – Water splitting and O2 generation How are 4 oxidising equivalents brought together at the OEC in Photosystem II and what is the current state of mimicking this centre? |
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NOVEL MATERIALS AND MICRODROPLETS (MM) (MM1) From Molecules to Materials (3L) The increasing need to develop low-temperature ‘soft’ approaches to existing or brand new materials presents the synthetic chemist with challenging and fresh horizons in the future. This short course will highlight how even simple inorganic and organic molecules, which have the right stoichiometry and characteristics, can be used to make electronic, catalytic and energy materials in a ‘bottom-up’ approach. The primary focus of the course is on the synthesis and design of precursors and the various epitaxial (vapour-phase) and solution approaches that have been used to deposit materials, comparing these approaches to high-temperature solid-state synthesis in particular. It will also describe how the array of modern solid-state methods can be used to characterise materials and how these materials function on a qualitative level in a number of key applications. |
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| Mon 20 |
Chemistry: Introduction to LaTeX
Finished
LaTeX is a computer program for automatically typesetting documents. Presentation is separated from content. At the end of the course you will be able to use latex to incorporate graphics, tables, sections, chapters, mathematical and chemical equations, internal cross references, a bibliography and a table of contents into a document. |
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NOVEL MATERIALS AND MICRODROPLETS (MM) (MM2) Conjugated polymers: Synthesis, Devices and Research Challenges (2L) Course Presented by Cambridge Display Technology The first of the lectures in this section will cover polymer organic light emitting diode materials and the new and exciting challenges these pose for synthetic organic chemists. The second will consider the route from organic materials synthesis to high performance solution processable electro-optical devices. |
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| Tue 21 |
Chemistry: Graduate Lecture Series: (BIO1) Protein Folding, Misfolding and Aggregation (8L)
Finished
BIOLOGICAL (BIO) (BIO1) Protein Folding, Misfolding and Aggregation (8L) AAN 1. Techniques to study protein structure and stability (Part II Recap) AAN 2. Techniques to study protein folding pathways (Part III Recap) These first two lectures will be based on the undergraduate protein courses, and will provide a general introduction to the field. Contents will include protein structure determination (NMR, X-ray crystallography, CD, FRET), protein stability calculations (chemical / thermal denaturation) and the characterisation of protein folding pathways and mechanisms (stopped-flow, hydrogen exchange, -values). AAN 3. Protein folding studies: simple systems AAN 4. Protein folding studies: more complex systems These two lectures will go beyond the undergraduate course, to look at how it is possible to use a multidisciplinary approach to elucidate detailed mechanistic information about protein folding pathways. Contents will include the study of knotted proteins, characterisation of misfolded proteins, the use of optical tweezers and AFM, the study of co-translational folding, and the identification of cooperativity in multidomain proteins. SEJ 5. Molecular chaperones: role in biological protein folding and misfolding SEJ 6. Molecular chaperones: therapeutic targets or therapeutic agents? These two lectures will start by discussing the important differences between protein folding in vitro and protein folding in vivo, and will highlight the need for biological chaperones and the consequences of chaperone disfunction. Contents will include details of ATP-independent chaperones, such as the heat shock proteins and the ATP-dependent chaperones, such as the GroEL/GroES complex. The lectures will finish by looking at the suppression of protein aggregation by natural chaperones and will discuss the possible therapeutic uses of this discovery. SLS 7. Intrinsically disordered proteins: structure and function SLS 8. Studying the coupled folding and binding of IDPS These final two lectures will look at a class of proteins that are natively unstructured but biologically active and thus appear to break the structure-function paradigm. Such proteins are not anomalies and indeed recent studies suggest that over 1/3 of proteins in eukaryotic organisms contain intrinsically disordered regions. These lectures will look at the possible reasons for disorder and will suggest why many such proteins are found to be signaling hubs. The course will finish by looking at techniques that can be used to study coupled folding and binding of these proteins and will emphasise the common flaws and misconceptions that hinder such kinetic studies. |
| Wed 22 |
Chemistry: Graduate Lecture Series: (BIO1) Protein Folding, Misfolding and Aggregation (8L)
Finished
BIOLOGICAL (BIO) (BIO1) Protein Folding, Misfolding and Aggregation (8L) AAN 1. Techniques to study protein structure and stability (Part II Recap) AAN 2. Techniques to study protein folding pathways (Part III Recap) These first two lectures will be based on the undergraduate protein courses, and will provide a general introduction to the field. Contents will include protein structure determination (NMR, X-ray crystallography, CD, FRET), protein stability calculations (chemical / thermal denaturation) and the characterisation of protein folding pathways and mechanisms (stopped-flow, hydrogen exchange, -values). AAN 3. Protein folding studies: simple systems AAN 4. Protein folding studies: more complex systems These two lectures will go beyond the undergraduate course, to look at how it is possible to use a multidisciplinary approach to elucidate detailed mechanistic information about protein folding pathways. Contents will include the study of knotted proteins, characterisation of misfolded proteins, the use of optical tweezers and AFM, the study of co-translational folding, and the identification of cooperativity in multidomain proteins. SEJ 5. Molecular chaperones: role in biological protein folding and misfolding SEJ 6. Molecular chaperones: therapeutic targets or therapeutic agents? These two lectures will start by discussing the important differences between protein folding in vitro and protein folding in vivo, and will highlight the need for biological chaperones and the consequences of chaperone disfunction. Contents will include details of ATP-independent chaperones, such as the heat shock proteins and the ATP-dependent chaperones, such as the GroEL/GroES complex. The lectures will finish by looking at the suppression of protein aggregation by natural chaperones and will discuss the possible therapeutic uses of this discovery. SLS 7. Intrinsically disordered proteins: structure and function SLS 8. Studying the coupled folding and binding of IDPS These final two lectures will look at a class of proteins that are natively unstructured but biologically active and thus appear to break the structure-function paradigm. Such proteins are not anomalies and indeed recent studies suggest that over 1/3 of proteins in eukaryotic organisms contain intrinsically disordered regions. These lectures will look at the possible reasons for disorder and will suggest why many such proteins are found to be signaling hubs. The course will finish by looking at techniques that can be used to study coupled folding and binding of these proteins and will emphasise the common flaws and misconceptions that hinder such kinetic studies. |
| Fri 24 |
Chemistry: Graduate Lecture Series: (BIO1) Protein Folding, Misfolding and Aggregation (8L)
Finished
BIOLOGICAL (BIO) (BIO1) Protein Folding, Misfolding and Aggregation (8L) AAN 1. Techniques to study protein structure and stability (Part II Recap) AAN 2. Techniques to study protein folding pathways (Part III Recap) These first two lectures will be based on the undergraduate protein courses, and will provide a general introduction to the field. Contents will include protein structure determination (NMR, X-ray crystallography, CD, FRET), protein stability calculations (chemical / thermal denaturation) and the characterisation of protein folding pathways and mechanisms (stopped-flow, hydrogen exchange, -values). AAN 3. Protein folding studies: simple systems AAN 4. Protein folding studies: more complex systems These two lectures will go beyond the undergraduate course, to look at how it is possible to use a multidisciplinary approach to elucidate detailed mechanistic information about protein folding pathways. Contents will include the study of knotted proteins, characterisation of misfolded proteins, the use of optical tweezers and AFM, the study of co-translational folding, and the identification of cooperativity in multidomain proteins. SEJ 5. Molecular chaperones: role in biological protein folding and misfolding SEJ 6. Molecular chaperones: therapeutic targets or therapeutic agents? These two lectures will start by discussing the important differences between protein folding in vitro and protein folding in vivo, and will highlight the need for biological chaperones and the consequences of chaperone disfunction. Contents will include details of ATP-independent chaperones, such as the heat shock proteins and the ATP-dependent chaperones, such as the GroEL/GroES complex. The lectures will finish by looking at the suppression of protein aggregation by natural chaperones and will discuss the possible therapeutic uses of this discovery. SLS 7. Intrinsically disordered proteins: structure and function SLS 8. Studying the coupled folding and binding of IDPS These final two lectures will look at a class of proteins that are natively unstructured but biologically active and thus appear to break the structure-function paradigm. Such proteins are not anomalies and indeed recent studies suggest that over 1/3 of proteins in eukaryotic organisms contain intrinsically disordered regions. These lectures will look at the possible reasons for disorder and will suggest why many such proteins are found to be signaling hubs. The course will finish by looking at techniques that can be used to study coupled folding and binding of these proteins and will emphasise the common flaws and misconceptions that hinder such kinetic studies. |
| Mon 27 |
NOVEL MATERIALS AND MICRODROPLETS (MM) (MM3) Artificial and Natural Materials: Properties, Manufacturing and Applications (3L) Nano-structured materials interact with light in unconventional ways: For example, it is possible to create brilliant and iridescent coloration using transparent materials or make invisibility cloaks using metals. Within this course, I will provide an overview on how light-propagation can be manipulated and tailored by nano-structuring materials. In particular, the first lecture will revise the basic principles of light-matter interaction and photonic crystals. The second lecture will focus on fabrication techniques and unresolved challenges for manufacturing of such materials on a large scale. In the last lecture, I will show how nature produces extremely complicated photonic structures (sometimes impossible to replicate artificially) on large-scale at room temperature using only simple materials like cellulose or chitin. |
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INTRODUCTORY LECTURES (IL) (IL1) Successful Completion of a Research Degree (previously entitled You and Your PhD: How to Write a Thesis) In this introductory session, time will be devoted to a discussion of how to plan your time effectively on a day to day basis, how to produce a dissertation/thesis and the essential requirements of an experimental section. General information will also be provided on the regulations and process surrounding submission of the first year probationary report and PhD thesis. |
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| Tue 28 |
Chemistry: Graduate Lecture Series: (BIO1) Protein Folding, Misfolding and Aggregation (8L)
Finished
BIOLOGICAL (BIO) (BIO1) Protein Folding, Misfolding and Aggregation (8L) AAN 1. Techniques to study protein structure and stability (Part II Recap) AAN 2. Techniques to study protein folding pathways (Part III Recap) These first two lectures will be based on the undergraduate protein courses, and will provide a general introduction to the field. Contents will include protein structure determination (NMR, X-ray crystallography, CD, FRET), protein stability calculations (chemical / thermal denaturation) and the characterisation of protein folding pathways and mechanisms (stopped-flow, hydrogen exchange, -values). AAN 3. Protein folding studies: simple systems AAN 4. Protein folding studies: more complex systems These two lectures will go beyond the undergraduate course, to look at how it is possible to use a multidisciplinary approach to elucidate detailed mechanistic information about protein folding pathways. Contents will include the study of knotted proteins, characterisation of misfolded proteins, the use of optical tweezers and AFM, the study of co-translational folding, and the identification of cooperativity in multidomain proteins. SEJ 5. Molecular chaperones: role in biological protein folding and misfolding SEJ 6. Molecular chaperones: therapeutic targets or therapeutic agents? These two lectures will start by discussing the important differences between protein folding in vitro and protein folding in vivo, and will highlight the need for biological chaperones and the consequences of chaperone disfunction. Contents will include details of ATP-independent chaperones, such as the heat shock proteins and the ATP-dependent chaperones, such as the GroEL/GroES complex. The lectures will finish by looking at the suppression of protein aggregation by natural chaperones and will discuss the possible therapeutic uses of this discovery. SLS 7. Intrinsically disordered proteins: structure and function SLS 8. Studying the coupled folding and binding of IDPS These final two lectures will look at a class of proteins that are natively unstructured but biologically active and thus appear to break the structure-function paradigm. Such proteins are not anomalies and indeed recent studies suggest that over 1/3 of proteins in eukaryotic organisms contain intrinsically disordered regions. These lectures will look at the possible reasons for disorder and will suggest why many such proteins are found to be signaling hubs. The course will finish by looking at techniques that can be used to study coupled folding and binding of these proteins and will emphasise the common flaws and misconceptions that hinder such kinetic studies. |
| Wed 29 |
NOVEL MATERIALS AND MICRODROPLETS (MM) (MM3) Artificial and Natural Materials: Properties, Manufacturing and Applications (3L) Nano-structured materials interact with light in unconventional ways: For example, it is possible to create brilliant and iridescent coloration using transparent materials or make invisibility cloaks using metals. Within this course, I will provide an overview on how light-propagation can be manipulated and tailored by nano-structuring materials. In particular, the first lecture will revise the basic principles of light-matter interaction and photonic crystals. The second lecture will focus on fabrication techniques and unresolved challenges for manufacturing of such materials on a large scale. In the last lecture, I will show how nature produces extremely complicated photonic structures (sometimes impossible to replicate artificially) on large-scale at room temperature using only simple materials like cellulose or chitin. |
| Thu 30 |
Chemistry: Graduate Lecture Series: (BIO1) Protein Folding, Misfolding and Aggregation (8L)
Finished
BIOLOGICAL (BIO) (BIO1) Protein Folding, Misfolding and Aggregation (8L) AAN 1. Techniques to study protein structure and stability (Part II Recap) AAN 2. Techniques to study protein folding pathways (Part III Recap) These first two lectures will be based on the undergraduate protein courses, and will provide a general introduction to the field. Contents will include protein structure determination (NMR, X-ray crystallography, CD, FRET), protein stability calculations (chemical / thermal denaturation) and the characterisation of protein folding pathways and mechanisms (stopped-flow, hydrogen exchange, -values). AAN 3. Protein folding studies: simple systems AAN 4. Protein folding studies: more complex systems These two lectures will go beyond the undergraduate course, to look at how it is possible to use a multidisciplinary approach to elucidate detailed mechanistic information about protein folding pathways. Contents will include the study of knotted proteins, characterisation of misfolded proteins, the use of optical tweezers and AFM, the study of co-translational folding, and the identification of cooperativity in multidomain proteins. SEJ 5. Molecular chaperones: role in biological protein folding and misfolding SEJ 6. Molecular chaperones: therapeutic targets or therapeutic agents? These two lectures will start by discussing the important differences between protein folding in vitro and protein folding in vivo, and will highlight the need for biological chaperones and the consequences of chaperone disfunction. Contents will include details of ATP-independent chaperones, such as the heat shock proteins and the ATP-dependent chaperones, such as the GroEL/GroES complex. The lectures will finish by looking at the suppression of protein aggregation by natural chaperones and will discuss the possible therapeutic uses of this discovery. SLS 7. Intrinsically disordered proteins: structure and function SLS 8. Studying the coupled folding and binding of IDPS These final two lectures will look at a class of proteins that are natively unstructured but biologically active and thus appear to break the structure-function paradigm. Such proteins are not anomalies and indeed recent studies suggest that over 1/3 of proteins in eukaryotic organisms contain intrinsically disordered regions. These lectures will look at the possible reasons for disorder and will suggest why many such proteins are found to be signaling hubs. The course will finish by looking at techniques that can be used to study coupled folding and binding of these proteins and will emphasise the common flaws and misconceptions that hinder such kinetic studies. |
May 2015
| Fri 1 |
Chemistry: Graduate Lecture Series: (BIO1) Protein Folding, Misfolding and Aggregation (8L)
Finished
BIOLOGICAL (BIO) (BIO1) Protein Folding, Misfolding and Aggregation (8L) AAN 1. Techniques to study protein structure and stability (Part II Recap) AAN 2. Techniques to study protein folding pathways (Part III Recap) These first two lectures will be based on the undergraduate protein courses, and will provide a general introduction to the field. Contents will include protein structure determination (NMR, X-ray crystallography, CD, FRET), protein stability calculations (chemical / thermal denaturation) and the characterisation of protein folding pathways and mechanisms (stopped-flow, hydrogen exchange, -values). AAN 3. Protein folding studies: simple systems AAN 4. Protein folding studies: more complex systems These two lectures will go beyond the undergraduate course, to look at how it is possible to use a multidisciplinary approach to elucidate detailed mechanistic information about protein folding pathways. Contents will include the study of knotted proteins, characterisation of misfolded proteins, the use of optical tweezers and AFM, the study of co-translational folding, and the identification of cooperativity in multidomain proteins. SEJ 5. Molecular chaperones: role in biological protein folding and misfolding SEJ 6. Molecular chaperones: therapeutic targets or therapeutic agents? These two lectures will start by discussing the important differences between protein folding in vitro and protein folding in vivo, and will highlight the need for biological chaperones and the consequences of chaperone disfunction. Contents will include details of ATP-independent chaperones, such as the heat shock proteins and the ATP-dependent chaperones, such as the GroEL/GroES complex. The lectures will finish by looking at the suppression of protein aggregation by natural chaperones and will discuss the possible therapeutic uses of this discovery. SLS 7. Intrinsically disordered proteins: structure and function SLS 8. Studying the coupled folding and binding of IDPS These final two lectures will look at a class of proteins that are natively unstructured but biologically active and thus appear to break the structure-function paradigm. Such proteins are not anomalies and indeed recent studies suggest that over 1/3 of proteins in eukaryotic organisms contain intrinsically disordered regions. These lectures will look at the possible reasons for disorder and will suggest why many such proteins are found to be signaling hubs. The course will finish by looking at techniques that can be used to study coupled folding and binding of these proteins and will emphasise the common flaws and misconceptions that hinder such kinetic studies. |
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NOVEL MATERIALS AND MICRODROPLETS (MM) (MM3) Artificial and Natural Materials: Properties, Manufacturing and Applications (3L) Nano-structured materials interact with light in unconventional ways: For example, it is possible to create brilliant and iridescent coloration using transparent materials or make invisibility cloaks using metals. Within this course, I will provide an overview on how light-propagation can be manipulated and tailored by nano-structuring materials. In particular, the first lecture will revise the basic principles of light-matter interaction and photonic crystals. The second lecture will focus on fabrication techniques and unresolved challenges for manufacturing of such materials on a large scale. In the last lecture, I will show how nature produces extremely complicated photonic structures (sometimes impossible to replicate artificially) on large-scale at room temperature using only simple materials like cellulose or chitin. |
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| Mon 4 |
DRUG DISCOVERY (DD) (I) (DD1) The Drug Discovery Process (2L) Drug discovery is a complex multidisciplinary process with chemistry as the core discipline. A small molecule New Chemical Entity (NCE) (80% of drugs marketed) has had its genesis in the mind of a chemist. A successful drug is not only biologically active (the easy bit), but is also therapeutically effective in the clinic – it has the correct pharmacokinetics, lack of toxicity, is stable and synthesisable in bulk, selective and can be patented. Increasingly, it must act at a genetically defined sub-population of patients. Medicinal chemists therefore work at the centre of a web of disciplines – biology, pharmacology, molecular biology, toxicology, materials science, intellectual property and medicine. This fascinating interplay of disciplines is the intellectual space within which a chemist has to make the key compound that will become an effective medicine. It happens rarely, despite enormous investment in time, money and effort. What factors make a program successful? I would like to briefly outline the process, but importantly to offer some key with examples of success. |
| Tue 5 |
DRUG DISCOVERY (DD) (I) (DD2) Agrochemical Discovery Course presented by Dr Steve Smith (Syngenta) As the world population continues to grow, so does the need to increase global food production sustainably with limited resources. Agrochemicals, in the form of herbicides, fungicides and insecticides, provide an important tool for farmers to combat the weeds, fungi and insect pests that target their crops and help to ensure reliable yields and quality produce. Resistance, emerging pests, abiotic stress and regulatory pressure all drive an ongoing search for new and more innovative crop protection products. This lecture will outline the process used to discover new agrochemicals, from lead generation through to development. It will show the critical roles that chemistry, biology and human & environmental safety play, illustrated with a number of recent examples. |
| Wed 6 |
DRUG DISCOVERY (DD) (I) (DD1) The Drug Discovery Process (2L) Drug discovery is a complex multidisciplinary process with chemistry as the core discipline. A small molecule New Chemical Entity (NCE) (80% of drugs marketed) has had its genesis in the mind of a chemist. A successful drug is not only biologically active (the easy bit), but is also therapeutically effective in the clinic – it has the correct pharmacokinetics, lack of toxicity, is stable and synthesisable in bulk, selective and can be patented. Increasingly, it must act at a genetically defined sub-population of patients. Medicinal chemists therefore work at the centre of a web of disciplines – biology, pharmacology, molecular biology, toxicology, materials science, intellectual property and medicine. This fascinating interplay of disciplines is the intellectual space within which a chemist has to make the key compound that will become an effective medicine. It happens rarely, despite enormous investment in time, money and effort. What factors make a program successful? I would like to briefly outline the process, but importantly to offer some key with examples of success. |
| Thu 7 |
DRUG DISCOVERY (DD) (I) (DD3) Targeted Anti-Cancer Therapeutics (2L) The targeted delivery of effector molecules into diseased tissues has emerged as a promising strategy for the treatment of cancer and other serious conditions. Linking a therapeutic effector (e.g. cytotoxics, proinflammatory cytokines or radionuclides) to a ligand specific to a marker of disease results in preferential accumulation of the effector molecule at the target tissue. This offers the double benefit of increased effective concentrations at the intended site of action and low concentrations in healthy tissues, thus reducing side effects. In the course of these two lectures we will discuss strategies for the discovery of selective ligands against markers of disease, conjugation chemistry in the context of drug-delivery strategies, and examples of recently approved FDA drug conjugates for the treatment of cancer. |
| Fri 8 |
DRUG DISCOVERY (DD) (I) (DD3) Targeted Anti-Cancer Therapeutics (2L) The targeted delivery of effector molecules into diseased tissues has emerged as a promising strategy for the treatment of cancer and other serious conditions. Linking a therapeutic effector (e.g. cytotoxics, proinflammatory cytokines or radionuclides) to a ligand specific to a marker of disease results in preferential accumulation of the effector molecule at the target tissue. This offers the double benefit of increased effective concentrations at the intended site of action and low concentrations in healthy tissues, thus reducing side effects. In the course of these two lectures we will discuss strategies for the discovery of selective ligands against markers of disease, conjugation chemistry in the context of drug-delivery strategies, and examples of recently approved FDA drug conjugates for the treatment of cancer. |
| Mon 11 |
CHARACTERISATION TECHNIQUES (CT) (CT6) Understanding NMR Spectroscopy (11L) By now you will be familiar with the use of NMR as a qualitative tool for structure determination, but little has been said so far about what NMR spectroscopy actually is and how it works. One of the beauties of NMR is that you can use it every day to help in identifying chemical structures without ever having to worry about what is actually going on in the experiment. However, there comes a time when either our curiosity, or our need to understand more deeply what we are doing, brings us to the point where we really want to know what NMR is. This is where this course fits in. The course starts out by considering the basic NMR experiment which, it turns out, is performed in rather a different way to virtually all other kinds of spectroscopy. Rather than looking for the absorption of radiation by the spins, we excite the spins with a short burst of radiation and then detect the ringing signal which is induced. The Fourier transform of this ringing signal is the familiar spectrum. In order to understand this most basic experiment we will have to develop the vector model, which is a precise semi-classical way of understanding the behaviour of the spins. Once we have the vector model we can begin to explore other experiments which involving pulses, including the famous spin echo experiment, which is the basis for many further developments. Useful though the vector model is, it is not able to describe the behaviour of coupled spins, and in particular the important phenomena of coherence transfer and multiple quantum coherence. To deal with these effects we need the quantum mechanical approach offered by the product operator method. We will not concern ourselves too much with where this theory comes from, but will find that it can be used in a simple and intuitive way to explain all of the important phenomena in modern NMR. In particular, we will be able to understand how two-dimensional experiments, with such delightful names as COSY, DQF-COSY and HMQC work. It is these experiment which have so revolutionized the application of NMR over the past twenty years. Time permitting, we will also look at relaxation in NMR spectroscopy. In contrast to most other kinds of spectroscopy, the excited states generated in pulsed NMR are very long-lived, and this means that it is relatively easy to study the way in which these states return to equilibrium – which is what relaxation is. The rate of relaxation gives important insight into molecular motion, and relaxation is also responsible for the nuclear Overhauser effect (NOE) which is an exceptionally important tool in structure determination by NMR. Recommended books: James Keeler Understanding NMR Spectroscopy , Wiley 2005 (The course will largely be based on this text) Hore, P. J., Nuclear Magnetic Resonance , OUP 1995. |
| Tue 12 |
CHARACTERISATION TECHNIQUES (CT) (CT6) Understanding NMR Spectroscopy (11L) By now you will be familiar with the use of NMR as a qualitative tool for structure determination, but little has been said so far about what NMR spectroscopy actually is and how it works. One of the beauties of NMR is that you can use it every day to help in identifying chemical structures without ever having to worry about what is actually going on in the experiment. However, there comes a time when either our curiosity, or our need to understand more deeply what we are doing, brings us to the point where we really want to know what NMR is. This is where this course fits in. The course starts out by considering the basic NMR experiment which, it turns out, is performed in rather a different way to virtually all other kinds of spectroscopy. Rather than looking for the absorption of radiation by the spins, we excite the spins with a short burst of radiation and then detect the ringing signal which is induced. The Fourier transform of this ringing signal is the familiar spectrum. In order to understand this most basic experiment we will have to develop the vector model, which is a precise semi-classical way of understanding the behaviour of the spins. Once we have the vector model we can begin to explore other experiments which involving pulses, including the famous spin echo experiment, which is the basis for many further developments. Useful though the vector model is, it is not able to describe the behaviour of coupled spins, and in particular the important phenomena of coherence transfer and multiple quantum coherence. To deal with these effects we need the quantum mechanical approach offered by the product operator method. We will not concern ourselves too much with where this theory comes from, but will find that it can be used in a simple and intuitive way to explain all of the important phenomena in modern NMR. In particular, we will be able to understand how two-dimensional experiments, with such delightful names as COSY, DQF-COSY and HMQC work. It is these experiment which have so revolutionized the application of NMR over the past twenty years. Time permitting, we will also look at relaxation in NMR spectroscopy. In contrast to most other kinds of spectroscopy, the excited states generated in pulsed NMR are very long-lived, and this means that it is relatively easy to study the way in which these states return to equilibrium – which is what relaxation is. The rate of relaxation gives important insight into molecular motion, and relaxation is also responsible for the nuclear Overhauser effect (NOE) which is an exceptionally important tool in structure determination by NMR. Recommended books: James Keeler Understanding NMR Spectroscopy , Wiley 2005 (The course will largely be based on this text) Hore, P. J., Nuclear Magnetic Resonance , OUP 1995. |
| Wed 13 |
This course covers the tips, tricks and techniques necessary to help your application and interview stand out from the crowd. You will be encouraged to step into the selector's shoes, and have your questions answered by a trained careers adviser. Students should consider attending Career Options BEFORE Applications and Selections. |
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DRUG DISCOVERY (DD) (I) (DD4) Fragment-based Drug Discovery (2L) Fragment-based approaches to finding novel small molecules that bind to proteins are now firmly established in drug discovery and chemical biology. Initially developed primarily in a few centres in the biotech and pharma industry, this methodology has now been adopted widely in both the pharmaceutical industry and academia. After the initial success with kinase targets, the versatility of this approach has now expanded to a broad range of different protein classes such as metalloproteins and protein-protein interactions. In the course of these two lectures we will explore the different strategies for finding a fragment hit and the subsequent elaboration strategies used in order to increase potency to develop a lead compound. |
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| Thu 14 |
CHARACTERISATION TECHNIQUES (CT) (CT6) Understanding NMR Spectroscopy (11L) By now you will be familiar with the use of NMR as a qualitative tool for structure determination, but little has been said so far about what NMR spectroscopy actually is and how it works. One of the beauties of NMR is that you can use it every day to help in identifying chemical structures without ever having to worry about what is actually going on in the experiment. However, there comes a time when either our curiosity, or our need to understand more deeply what we are doing, brings us to the point where we really want to know what NMR is. This is where this course fits in. The course starts out by considering the basic NMR experiment which, it turns out, is performed in rather a different way to virtually all other kinds of spectroscopy. Rather than looking for the absorption of radiation by the spins, we excite the spins with a short burst of radiation and then detect the ringing signal which is induced. The Fourier transform of this ringing signal is the familiar spectrum. In order to understand this most basic experiment we will have to develop the vector model, which is a precise semi-classical way of understanding the behaviour of the spins. Once we have the vector model we can begin to explore other experiments which involving pulses, including the famous spin echo experiment, which is the basis for many further developments. Useful though the vector model is, it is not able to describe the behaviour of coupled spins, and in particular the important phenomena of coherence transfer and multiple quantum coherence. To deal with these effects we need the quantum mechanical approach offered by the product operator method. We will not concern ourselves too much with where this theory comes from, but will find that it can be used in a simple and intuitive way to explain all of the important phenomena in modern NMR. In particular, we will be able to understand how two-dimensional experiments, with such delightful names as COSY, DQF-COSY and HMQC work. It is these experiment which have so revolutionized the application of NMR over the past twenty years. Time permitting, we will also look at relaxation in NMR spectroscopy. In contrast to most other kinds of spectroscopy, the excited states generated in pulsed NMR are very long-lived, and this means that it is relatively easy to study the way in which these states return to equilibrium – which is what relaxation is. The rate of relaxation gives important insight into molecular motion, and relaxation is also responsible for the nuclear Overhauser effect (NOE) which is an exceptionally important tool in structure determination by NMR. Recommended books: James Keeler Understanding NMR Spectroscopy , Wiley 2005 (The course will largely be based on this text) Hore, P. J., Nuclear Magnetic Resonance , OUP 1995. |
| Fri 15 |
DRUG DISCOVERY (DD) (I) (DD4) Fragment-based Drug Discovery (2L) Fragment-based approaches to finding novel small molecules that bind to proteins are now firmly established in drug discovery and chemical biology. Initially developed primarily in a few centres in the biotech and pharma industry, this methodology has now been adopted widely in both the pharmaceutical industry and academia. After the initial success with kinase targets, the versatility of this approach has now expanded to a broad range of different protein classes such as metalloproteins and protein-protein interactions. In the course of these two lectures we will explore the different strategies for finding a fragment hit and the subsequent elaboration strategies used in order to increase potency to develop a lead compound. |