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Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures.


ABSTRACT: Progressive structuring and ultimately exclusion of water by hydrophobes surrounding backbone hydrogen bonds turn the latter into guiding factors of protein folding. Here we demonstrate that an arrangement of five hydrophobes yields an optimal hydrogen-bond stabilization. This motif is shown to be nearly ubiquitous in native folds.

SUBMITTER: Fernandez A 

PROVIDER: S-EPMC1302333 | biostudies-other | 2002 Nov

REPOSITORIES: biostudies-other

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Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures.

Fernández Ariel A   Berry R Stephen RS  

Biophysical journal 20021101 5


Progressive structuring and ultimately exclusion of water by hydrophobes surrounding backbone hydrogen bonds turn the latter into guiding factors of protein folding. Here we demonstrate that an arrangement of five hydrophobes yields an optimal hydrogen-bond stabilization. This motif is shown to be nearly ubiquitous in native folds. ...[more]

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