By László Patthy
This ebook presents an updated precis of the foundations of protein evolution and discusses either the equipment on hand to research the evolutionary historical past of proteins in addition to these for predicting their structure-function relationships. * contains a considerably extended bankruptcy on genome evolution to hide genomes of version organisms sequenced because the final touch of the 1st variation, and organelle genome evolution * keeps its reader-friendly, obtainable variety and association * includes an up to date thesaurus and new references, together with a listing of on-line reference websites
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Extra resources for Protein Evolution (2nd Edition)
Qxd 10/08/2007 10:06 AM Page 29 PROTEIN STRUCTURE 29 The importance of interaction between partial charges may be best illustrated by the peptide bond, which has partially double-bonded character due to resonance with a form in which the more electronegative oxygen atom acquires a net partial negative charge, whereas the –NH– group has a partial positive charge. The importance of electrostatic interactions between partial charges may also be illustrated by the side chains of Phe, Tyr and Trp residues.
G. zinc enzymes). Phenylalanine, tyrosine and tryptophan These bulky hydrophobic amino acid residues interact more favourably with each other and with other nonpolar amino acids (aliphatic amino acids) than with water. This ‘hydrophobic interaction’ is one of the main factors that stabilize the folded conformations of proteins: the aromatic residues frequently form the cores of protein folds. The aromatic ring of phenylalanine is unreactive, however, the hydroxyl group of the phenolic ring of tyrosine residues makes this aromatic ring relatively reactive.
1995) Proteins with leucinerich repeats. ) Reprinted from Current Opinion in Structural Biology, 5, Kobe, B. , Proteins with leucine-rich repeats, 409– 416, Copyright 1995, with permission from Elsevier. located in the cavity. The α-helices line the outer surface of the horseshoe; the β-strands form a parallel β-sheet along its inner surface (Fig. 1). LRR proteins are widespread, being present in all types of organisms, including bacteria, yeast, plants and animals. Moreover, they are found in the cytoplasm as well as in extracellular proteins, and show functional versatility: they occur in proteins involved in signal transduction, cell adhesion, development, DNA repair, recombination, transcription and RNA processing.