Barbara Mulloy – författare

The three volumes in Methods in Molecular Biology covering Physical Methods of Analysis (vol. 1, Spectroscopic Methods and Analyses: NMR, Mass Spectrometry, and Metalloprotein Techniques; vol. 2, Optical Spectroscopy and Macroscopic Techniques; vol. 3, Cryst- lographic Methods and Techniques) differ from others in this series in several ways. Each volume covers a group of techniques for the char- terization of biological molecules and their interactions that involve the application of modern techniques of physical chemistry. These techniques by and large do not lend themselves to the "hands-on" approach and cannot usually be carried out by the molecular biologist alone, but most often require collaboration with a specialist. The biologist or biochemist contemplating such a collaboration may feel somewhat at a distance from the experimental work and further isolated by the use of the jargons of analytical and physical chemistry. Physical methods have been used in molecular biology from the earliest days, from simple applications of optical spectroscopy to the complexity of X-ray crystallography, and the full range of these me- ods will be covered over the three volumes. The methods dealt with in this first volume have largely developed from beginnings in small molecule chemistry to the point where they play a valuable role in the characterization of biological macromolecules.

This is the second of three volumes of Methods in Molecular Biology that deal with Physical Methods of Analysis. The first of these, Spectroscopic Methods and Analyses dealt with NMR spec­ troscopy, mass spectrometry, and metalloprotein techniques, and the third will cover X-ray crystallographic methods. As with the first volume. Microscopy, Optical Spectroscopy, and Macroscopic Techniques is intended to provide a basic understand­ ing for the biochemist or biologist who needs to collaborate with spe­ cialists in applying the techniques of modern physical chemistry to biological macromolecules. The methods treated in this book fall into four groups. Part One covers microscopy, which aims to visualize individual molecules or complexes of several molecules. Electron microscopy is the more familiar of these, while scanning tunneling microscopy is a new and rapidly developing tool. Methods for determining the shapes and sizes of molecules in solution are described in Part Two, which includes chapters on X-ray and neutron scattering, light scattering, and ult- centrifugation. Calorimetry, described in Part Three, provides the means to monitor processes involving thermodynamic changes, whether these are intramolecular, such as conformational transition, or the interactions between solutes or between a solute and its sol­ vent. Part Four is concerned with optical and infrared spectroscopy and describes applications ranging from the measurement of protein concentration by UV absorbance to the analysis of secondary struc­ ture using circular dichroism and Fourier-transform infrared spec­ troscopy.

This is the second of three volumes of Methods in Molecular Biology that deal with Physical Methods of Analysis. The first of these, Spectroscopic Methods and Analyses dealt with NMR spec­ troscopy, mass spectrometry, and metalloprotein techniques, and the third will cover X-ray crystallographic methods. As with the first volume. Microscopy, Optical Spectroscopy, and Macroscopic Techniques is intended to provide a basic understand­ ing for the biochemist or biologist who needs to collaborate with spe­ cialists in applying the techniques of modern physical chemistry to biological macromolecules. The methods treated in this book fall into four groups. Part One covers microscopy, which aims to visualize individual molecules or complexes of several molecules. Electron microscopy is the more familiar of these, while scanning tunneling microscopy is a new and rapidly developing tool. Methods for determining the shapes and sizes of molecules in solution are described in Part Two, which includes chapters on X-ray and neutron scattering, light scattering, and ult- centrifugation. Calorimetry, described in Part Three, provides the means to monitor processes involving thermodynamic changes, whether these are intramolecular, such as conformational transition, or the interactions between solutes or between a solute and its sol­ vent. Part Four is concerned with optical and infrared spectroscopy and describes applications ranging from the measurement of protein concentration by UV absorbance to the analysis of secondary struc­ ture using circular dichroism and Fourier-transform infrared spec­ troscopy.

The three volumes in Methods in Molecular Biology covering Physical Methods of Analysis (vol. 1, Spectroscopic Methods and Analyses: NMR, Mass Spectrometry, and Metalloprotein Techniques; vol. 2, Optical Spectroscopy and Macroscopic Techniques; vol. 3, Cryst- lographic Methods and Techniques) differ from others in this series in several ways. Each volume covers a group of techniques for the char- terization of biological molecules and their interactions that involve the application of modern techniques of physical chemistry. These techniques by and large do not lend themselves to the "hands-on" approach and cannot usually be carried out by the molecular biologist alone, but most often require collaboration with a specialist. The biologist or biochemist contemplating such a collaboration may feel somewhat at a distance from the experimental work and further isolated by the use of the jargons of analytical and physical chemistry. Physical methods have been used in molecular biology from the earliest days, from simple applications of optical spectroscopy to the complexity of X-ray crystallography, and the full range of these me- ods will be covered over the three volumes. The methods dealt with in this first volume have largely developed from beginnings in small molecule chemistry to the point where they play a valuable role in the characterization of biological macromolecules.

This is the second of three volumes of Methods in Molecular Biology that deal with Physical Methods of Analysis. The first of these, Spectroscopic Methods and Analyses dealt with NMR spec­ troscopy, mass spectrometry, and metalloprotein techniques, and the third will cover X-ray crystallographic methods. As with the first volume. Microscopy, Optical Spectroscopy, and Macroscopic Techniques is intended to provide a basic understand­ ing for the biochemist or biologist who needs to collaborate with spe­ cialists in applying the techniques of modern physical chemistry to biological macromolecules. The methods treated in this book fall into four groups. Part One covers microscopy, which aims to visualize individual molecules or complexes of several molecules. Electron microscopy is the more familiar of these, while scanning tunneling microscopy is a new and rapidly developing tool. Methods for determining the shapes and sizes of molecules in solution are described in Part Two, which includes chapters on X-ray and neutron scattering, light scattering, and ult- centrifugation. Calorimetry, described in Part Three, provides the means to monitor processes involving thermodynamic changes, whether these are intramolecular, such as conformational transition, or the interactions between solutes or between a solute and its sol­ vent. Part Four is concerned with optical and infrared spectroscopy and describes applications ranging from the measurement of protein concentration by UV absorbance to the analysis of secondary struc­ ture using circular dichroism and Fourier-transform infrared spec­ troscopy.

The volumes in the series, Methods in Molecular Biology, are conceived with the biochemist and molecular biologist in mind. The present book, Crystallographic Methods andProtocols, concentrates on the use of X-ray crystallography to solve the detailed three­ dimensional structuresofproteins, nucleic acids, andtheir complexes. Such a structure determination is a major undertaking, demands expertise in a range of skills, and requires considerable resources. The biologically trained worker will probably first become involved when identifying an important scientific problem whose solution would benefit from a full structure. The protein or nucleic acid at issue must be sequenced and prepared to high purity in appropriate quantities, probably by either chemical synthesis for nucleic acids or genetic engineering for proteins. CrystallographicMethods andPro­ tocols aims to give biologically trained workers an insight into the techniques used to crystallize their proteins, obtain the raw X-ray data, and solve and refine the structure. The aim ofa crystal structure determination is to provide infor­ mation that will solve biologically relevant problems; that process normally requires a high resolution structure. The preparationofsuit­ able crystals for a high resolution structure remains the major bottle­ neck in structure determination, and the effective application of appropriate genetic engineering and biochemical techniques in the initial stages pays ahandsome dividend later. The productionofsuit­ able proteins by recombinant methods and the preparationofcrystal­ line derivatives are covered by Skelly and Madden in Chapter 2. Before beginning the data collection required for a high resolution structure, a preliminary characterizationofthe crystals is carried out.

Heparins remain amongst the most commonly used drugs in clinical practice.  Almost 100 years have passed since the initial discovery of this complex substance and, during this time, understanding of the nature and uses of heparin and related molecules has grown dramatically. The aim of this volume is to summarise the developments that have led to the current status of both heparins as drugs and the field of heparin research, with a focus on the particularly rapid progress that has been made over the past three decades. Individual sections are dedicated to the nature of heparin as a biological molecule, the current approaches and techniques that are used to ensure the safety and reliability of heparin as a medicine, the clinical pharmacology of heparin as an anticoagulant drug, effects and potential applications of heparin aside of those involving haemostasis and, finally, the nature and potential uses of heparin-like materials from both natural and synthetic sources.