ISSN:
1573-4943
Keywords:
protein secondary structure
;
structural classification of proteins
;
protein evolution
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Distributions of α and β regions in globular proteins among clusters containing different numbers of adjacent α-helices, adjacent β regions, and “overlapping” βαβ units are considered. It is shown that these distributions do not differ greatly from what can be expected for random distributions of α and β regions along protein chains. In particular, it is shown that the amounts of relatively long α, β and βαβ clusters (which provide the basis for the conventional classification of globular proteins or domains into α, β, or α/β types) in random sequences also do not differ very much from those in real globular proteins. It follows that the possibility of structural classification of globular proteins (domains) does not imply the existence of a correlation in protein primary structure. This possibility exists even in random sequences of amino acid residues and therefore may not be the result of biological evolution.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01025418
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