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A study of four-helix bundles: investigating protein folding via similar architectural motifs in protein cores and in subunit interfaces.

Abstract：

:Four-helix bundles are identified and characterized in the subunit interfaces of protein multimers. We find that this motif occurs as often in the interfaces as in the protein monomers. Common and different characteristics demonstrated by the bundles in the two environments suggest the possible stabilization mechanisms of the bundles via cooperative helical twist, dipole alignment and interhelical connections. Nucleation of parallel helix pairs may be a favourable pathway before the pairs couple into bundles during folding. Certain properties found chaotic in the interface four-helix bundles indicate that either the subunit association is far from the global minimum conformation, or that the footprints of the folding pathway are recorded in these properties.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Lin SL,Tsai CJ,Nussinov R

doi

10.1006/jmbi.1995.0208

subject

Has Abstract

pub_date

1995-04-21 00:00:00

pages

151-61

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(85)70208-2

journal_volume

248

pub_type

杂志文章

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