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Article

The role of plastic beta-hairpin and weak hydrophobic core in the stability and unfolding of a full sequence design protein.

The Journal of chemical physics - 15 Dec 2004

Lei Hongxing, Duan Yong

Abstract excerpt

In this study, the thermal stability of a designed alpha/beta protein FSD (full sequence design) was studied by explicit solvent simulations at three moderate temperatures, 273 K, 300 K, and 330 K. The average properties of the ten trajectories at each temperature were analyzed. The thermal unfolding, as judged by backbone root-mean-square deviation and percentage of native contacts, was displayed with increased...

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Identifiers

PMID: 15634176
DOI: 10.1063/1.1822916

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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