Sequence space, folding and protein design.

Abstract:

:Protein design efforts are beginning to yield molecules with many of the properties of natural proteins. Such experiments are informed by and contribute to our understanding of the sequence determinants of protein folding and stability. The most important design elements seem to be the proper placement of hydrophobic residues along the polypeptide chain and the ability of these residues to form a well packed core. Buried polar interactions, turn and capping motifs and secondary structural propensities also contribute, although probably to a lesser extent.

journal_name

Curr Opin Struct Biol

authors

Cordes MH,Davidson AR,Sauer RT

doi

10.1016/s0959-440x(96)80088-1

subject

Has Abstract

pub_date

1996-02-01 00:00:00

pages

3-10

issue

1

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(96)80088-1

journal_volume

6

pub_type

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