Biophysical Chemistry (Tutorial Chemistry Texts) - Softcover

Cooper, Alan

Softcover

ISBN 10: 1849730814 ISBN 13: 9781849730815

Publisher: Royal Society of Chemistry, 2011

Synopsis

Biophysical Chemistry covers the physical chemistry of biological macromolecules and the experimental techniques used to study them. Topics covered include: an introduction to biological molecules; spectroscopy, mass spectrometry and hydrodynamics of macromolecules; a ""bluffer's guide"" to molecular thermodynamics; biomolecular kinetics; chromatography and electrophoresis; and single-molecule methods. The easily digestible, pragmatic approach captures the reader with the fascinating challenges the subject poses for theoretical and experimental scientists. This book will be ideal for early undergraduates studying chemical or physical sciences and will act as a basis for more advanced study. Students in other areas of biological sciences will appreciate the less intimidating approach to physical chemistry as demonstrated here. Ideal for the needs of undergraduate chemistry students, Tutorial Chemistry Texts is a major series consisting of short, single topic or modular texts concentrating on the fundamental areas of chemistry taught in undergraduate science courses. Each book provides a concise account of the basic principles underlying a given subject, embodying an independent-learning philosophy and including worked examples.

About this title

About the Author

Alan Cooper is a Professor of Biophysical Chemistry in the Chemistry Department at Glasgow University, Glasgow, UK. After obtaining a first class honours degree in physics from Manchester University, he gained a diploma for Advanced Studies in Science (with Distinction) on the calculation of dispersion forces and optical properties of helical polynucleotides and a PhD in Biophysics on the thermodynamics of assembly and stability of collagen - both from Manchester University. Since then he has been a SRC Research Fellow at the Laboratory of Molecular Biophysics, Oxford University and a Junior Research Fellow, Wolfson College, Oxford as well as a NIH Research Fellow on the Pathology of Membranes Training Program in the department of Chemistry, Yale University, USA, before his return to Glasgow University as a Lecturer in Physical Chemistry, then Senior Lecturer, Reader and finally Professor. Until 2009, he was the Principal Editor of the Biophysical Chemistry journal and is on the Editorial boards of the European Biophysics Journal, Journal of the Iranian Chemical Society and BMC Biochemistry. He is an external assessor for various European universities and a member of the Molecular Biosciences Foresight Working Party, the ESF Working Party on post-genome biophysical studies and is on the management committee of COST D22 protein-lipid interaction. His research interests include biophysical chemistry, microcalorimetry; thermodynamics of protein folding, misfolding, aggregation and interactions; biomaterials chemistry, protein foams, nematode polyproteins; peptide-antibiotic interactions, and he has also had over 150 full papers published.

From the Back Cover

This fully revised and expanded second edition of a highly popular book covers the physical chemistry of biological macromolecules and how this may be studied using up-to-date instrumental techniques. The experimental approach used here reflects the way science actually works, especially in a developing field that does not yet have the rigorous theoretical understanding sometimes found in more mature areas of chemistry. This makes biophysical chemistry both fascinating and fun, posing interesting challenges for both theoretical and experimental scientists. This updated edition includes a new chapter on diffraction and microscopy, covering recent developments in a range of biomolecular imaging techniques. The section on circular dichroism has been fully revised to conform to more up-to-date convention and the section on multi-dimensional NMR has been enhanced. These revisions give the student an overview of the range of techniques available, together with the underlying physical basis, sufficient to act as a platform for more detailed treatment elsewhere. Other updates include recent developments arising from genome projects and a new section on foams and surfactants reflecting recent advances in biofoams, with topical marginal notes and a brief explanation of surface tension. The note about units has been expanded to include other commonly used non-SI units (eg the calorie). The "References" and "Further Reading" sections have been updated for all chapters and the marginal notes revised and amended, with new background material added where appropriate. The level adopted in this tutorial text is suitable for early undergraduate years in chemical or physical sciences. However, since this interdisciplinary topic is often postponed to later years, the book can also act as a basis for more advanced study. Students in other areas of the biological sciences will also appreciate the less intimidating approach to physical chemistry in the book.

Excerpt. © Reprinted by permission. All rights reserved.

Biophysical Chemistry

By Alan Cooper

The Royal Society of Chemistry

Copyright © 2011 A. Cooper
All rights reserved.

ISBN: 978-1-84973-081-5

Contents

1 Biological Molecules, 
2 Spectroscopy, 
3 Mass Spectrometry, 
4 Hydrodynamics, 
5 Thermodynamics and Interactions, 
6 Kinetics, 
7 Chromatography and Electrophoresis, 
8 Imaging, 
9 Single Molecules, 
Answers to Problems, 
Subject Index, 

CHAPTER 1

Biological Molecules

You don't need to know any biology in order to study biological molecules, but it does help to have some background.

1.1 Introduction

This book is mainly about the experimental methods used to understand the physical properties and function of the molecules that make up living systems.

These molecules — proteins, polynucleotides, polysaccharides, lipids — are not necessarily any different from molecules we study in other branches of chemistry. But there are some additional factors, arising from their biological origin, which we need to be aware of.

• Biological macromolecules are large molecules formed from many smaller units and are (usually) polymers of precise length and specific sequence.

• They (usually) fold or associate into specific conformational assemblies stabilized by non-covalent interactions.

• This (usually) happens in water.

• The molecules are the (usually) successful outcomes of biological evolution.

It is this last point that makes things so exciting for the biophysical chemist. The molecules we see today are the results of countless random (more or less) experiments over millions of years during which living systems have evolved to take advantage of subtle principles of physical chemistry that we barely yet understand. By studying such systems we can learn much about physical chemistry in general, with potential for applications in other areas.

1.2 Proteins and Polypeptides

Proteins are polymers made up of specific sequences of L-amino acids linked together by covalent peptide (amide) bonds (Figure 1.1). Amino acids are chosen from a basic set of 20 building blocks differing in side chain (Figure 1.2), with occasional special purpose side chains made to order (e.g. hydroxyproline).

D-amino acids are encountered only in special instances such as bacterial cell walls and peptide antibiotics.

Typical proteins range in polypeptide chain length from around 50 to 5000 amino acids. The average relative molecular mass of an amino acid is around 110, so proteins can have RMMs from 500 to 500 000 (0.5–500 kDa) or more — especially in multi-subunit proteins consisting of specific aggregates (see Table 1.1).

The term 'molecular weight' is not strictly accurate (why?) but is commonly used, especially in the older (biochemical) literature. The more correct terms are 'relative molecular mass (RMM)' (no units) or 'molar mass' (kg mol1 or g mol1). One dalton (1 Da) is equal to 1 amu (atomic mass unit).

Proteins function as enzymes (biological catalysts), antibodies, messengers, carriers, receptors, structural units, etc. Their chemical structure and molecular conformation are commonly described in terms of:

Primary structure: the sequence of amino acids in the polypeptide chain (see Figure 1.3). This is unique to each protein, and is determined (primarily) by the genetic information encoded in the DNA of the relevant gene.

Secondary structure: regular, repeating structures such as α-helix, β-sheets, etc. (see

Edition details

• Publisher: Royal Society of Chemistry
• Publication date: 2011
• Language: English
• ISBN 10: 1849730814
• ISBN 13: 9781849730815
• Binding: Paperback
• Edition number: 2
• Number of pages: 244