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Article

Conformational entropy of alanine versus glycine in protein denatured states.

Proceedings of the National Academy of Sciences of the United States of America - 20 Feb 2007

Scott Kathryn A, Alonso Darwin O V, Sato Satoshi, Fersht Alan R, Daggett Valerie

Abstract excerpt

The presence of a solvent-exposed alanine residue stabilizes a helix by 0.4-2 kcal.mol(-1) relative to glycine. Various factors have been suggested to account for the differences in helical propensity, from the higher conformational freedom of glycine sequences in the unfolded state to hydrophobic and van der Waals' stabilization of the alanine side chain in the helical state. We have performed all-atom molecular...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17307875
DOI: 10.1073/pnas.0611182104
PMCID: PMC1815238

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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