rotein folding is one of the great unsolved problems in biochemistry. This short textbook first reviews the protein structures that affect folding, then covers the thermodynamics and reaction kinetics. These are all topics familiar to most biochemists and enzymologists. After this, the book describes instrumentation useful in studying ultrafast denaturation and renaturation kinetics, including temperature jumps, protein engineering, fluorescence, and time-resolved circular dichroism and NMR. The remaining chapters discuss experimental problems such as aggregation and low protein expression levels, and specific examples using barstar, which is a 10 kDa ribonuclease inhibitor. Computer modeling and software are barely discussed; the software that is used (Molscript, etc.) is mostly old-fashioned, but still useful. Most of the references are from 1991 to 1996. The last chapter briefly describes the author's evolution folding simulation software. Although the long strings of references in "Name et al., year" format scattered on almost every page almost kill this book's readability, it is still a useful introduction to the methods of studying folding kinetics.
jan 21, 2012
his introductory textbook surveys some of the methods used in biophysics, the study of the physical properties of biomolecules. Chapters include mass spectrometry, X-ray crystallography, electron microscopy, de novo peptide sequencing, protein infrared spectroscopy, and a few other well-established techniques. A few relatively new techniques, including ion mobility spectrometry and nanotechnology, are also included. The coverage is light and relatively superficial, with some chapters only a few pages long. The author is a non-native English speaker, with all that that implies. One annoyance is that references are in "Name et al., year" format; many paragraphs are little more than a long string of references, making the book unpleasant to read. This book might be useful for non-specialists interested in an overview of the field, but it would be of very limited value for grad students or professional biophysicists seeking in-depth understanding.
jan 18, 2010
his textbook describes differential scanning calorimetry as used in industry to study inorganics and pure materials. The authors thoroughly describe instrument calibration, desmearing, and performance evaluation. There is also a chapter on using a DSC to measure reaction kinetics. The treatment leans toward the abstract, with little attention to data interpretation or the physical and chemical processes in the sample. There is no discussion of the use of DSC to study biomolecules, or of the problems with aqueous samples. The statement on the back cover that this book "enables researchers to select the best instrument" is untrue: the only mention of a physical device is an occasional vague reference to Perkin-Elmer, which is only one of many manufacturers. The authors are coy about what DSC is actually good for: it is not until page 238 that the authors finally get around to saying what information is obtained from temperature-modulated DSC (TMDSC). For those interested in the basic theory, the exposition is clear and easy to follow. Students looking for a practical introduction on how to run samples and interpret the results, readers interested in building or purchasing a machine, and researchers interested in biomolecules should look elsewhere ... like, maybe, the manual that came with their machine.
aug 1, 2010