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The four‐lielix bundle: what determines a fold?
Author(s) -
Kamtekar Satwik,
Hecht Michael H.
Publication year - 1995
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.9.11.7649401
Subject(s) - helix bundle , bundle , crystallography , protein folding , chemistry , structural motif , motif (music) , fold (higher order function) , coiled coil , protein structure , biophysics , physics , biology , biochemistry , computer science , materials science , acoustics , composite material , programming language
The four‐helix bundle motif occurs in many structural contexts and in proteins that are functionally diverse. The motif can be classified into individual folds on the basis of topological and geometric properties. It has been thoroughly investigated structurally by both nuclear magnetic resonance and x‐ray crystallography. Many mutants of four‐helix bundles have been generated, and the motif has also been the target of de novo design studies. Taken together, these studies provide an opportunity to examine many of the forces governing protein folding. In this article we consider the relative importance of the burial of hydrophobic residues, loss of conformational entropy, packing interactions, interhelical turn composition, and helical dipole interactions all within the context of a single folding motif. We conclude by examining why de novo designed fourhelix bundle proteins possess flexible interiors, and possible mechanisms by which natural proteins may lock their cores into rigid structures.—Kamtekar, S., Hecht, M. H. The four‐helix bundle: what determines a fold? FASEB J. 9, 1013‐1022 (1995)