Analysis of protein sequence/structure similarity relationships.

Abstract:

:Current analyses of protein sequence/structure relationships have focused on expected similarity relationships for structurally similar proteins. To survey and explore the basis of these relationships, we present a general sequence/structure map that covers all combinations of similarity/dissimilarity relationships and provide novel energetic analyses of these relationships. To aid our analysis, we divide protein relationships into four categories: expected/unexpected similarity (S and S(?)) and expected/unexpected dissimilarity (D and D(?)) relationships. In the expected similarity region S, we show that trends in the sequence/structure relation can be derived based on the requirement of protein stability and the energetics of sequence and structural changes. Specifically, we derive a formula relating sequence and structural deviations to a parameter characterizing protein stiffness; the formula fits the data reasonably well. We suggest that the absence of data in region S(?) (high structural but low sequence similarity) is due to unfavorable energetics. In contrast to region S, region D(?) (high sequence but low structural similarity) is well-represented by proteins that can accommodate large structural changes. Our analyses indicate that there are several categories of similarity relationships and that protein energetics provide a basis for understanding these relationships.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Gan HH,Perlow RA,Roy S,Ko J,Wu M,Huang J,Yan S,Nicoletta A,Vafai J,Sun D,Wang L,Noah JE,Pasquali S,Schlick T

doi

10.1016/s0006-3495(02)75287-9

subject

Has Abstract

pub_date

2002-11-01 00:00:00

pages

2781-91

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(02)75287-9

journal_volume

83

pub_type

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