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From The CriticsReviewer: Eugene A Davidson, PhD (Georgetown University School of Medicine)
Description: Ever since the revelatory work by Anfinsen on the refolding of ribonuclease, it has been the prevailing dogma that the final three-dimensional architecture of a protein is defined by its amino acid sequence. As a result, a large number of investigators have devoted themselves to the "folding problem." There are two aspects to this — how to predict the three dimensional structure from the amino acid sequence, and what mechanisms are employed by nascent protein to search conformational space for the right shape. The latter is the topic of this book.
Purpose: The purpose is to review current ideas of the mechanisms of protein folding. This worthy objective has been met by the author.
Audience: The intended audience is fellows and undergraduate and graduate students.
Features: An initial discussion of the folding problem itself is followed by chapters that discuss current views on kinetic approaches, early intermediates, and transition states including the molten globule. Methods for analysis of these transitions are reviewed including the use of NMR and mass spectrometry (both involving hydrogen exchange) as well as the role of what are thought to be slower processes such as proline isomerization and the formation of disulfide bonds. Several explicit examples are analyzed in detail (collagen triple helix, apomyoglobin); the book concludes with a brief discussion of chaperones and implications for aberrant protein folding in disease states. The chapters are all written by authorities in the area and each is accompanied by a useful bibliography.
Assessment: Although this is a second edition, it can reasonably be assumed that iterations will follow. Investigators working in the area will profit from the material covered as will graduate students and fellows.