Protein Structure and Function
Protein Structure and Function
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Pascal Gagneux
University of California, San Diego
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The Journal of Heredity 2004:95(3)
remarkably little sequence identity, effectively limiting the their organism of choice. The overview provided by the
usefulness of homology modeling. magnificent tables, be they on various quaternary structures,
One criticism I have is the exceedingly short treatment of protein domain interactions, or time and distance scales in
phylogenetic methods. Considering the importance of phy- functional genomics, will be worth going back to whenever
logenetics in comparative genomics, I would have expected panoramic orientation is needed.
the authors to at least mention the different methods of I particularly appreciated that throughout the book,
reconstructing evolutionary history (not just distance based, proteins are discussed within an evolutionary perspective,
but also maximum-likelihood methods using detailed discussing examples of convergent evolution, and addressing
probabilistic models of sequence evolution). gene evolution by domain rearrangement, notions of a past
The last chapter presents a very brief, but equally clear ‘‘RNA world’’ reflected in the persistence of RNA
explanation of the methods used for empirically elucidating coenzymes, and the differences in complexity between
protein structures, X-ray crystallography, and nuclear mag- prokaryotes and eukaryotes. Similarly the authors remind us
netic resonance (NMR). The limitations of each method are that proteins are part of evolving organisms by repeatedly
discussed, as well as factors potentially leading to erroneous addressing the complex spatial and temporal relationships
structure determination. The book provides a wealth of between the large number of differently modified proteins in
information and succeeds in keeping the reader’s attention and on living cells.
through the use of concise text and splendid graphics. Much can be learned from viewing functional, properly
Conveniently, the many definitions presented at the bottom folded proteins as precarious, ‘‘semiliquid’’ thermodynamic
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