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Article

Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar.

Proceedings of the National Academy of Sciences of the United States of America - 7 Jul 2015

Baxa Michael C, Yu Wookyung, Adhikari Aashish N, Ge Liang, Xia Zhen, Zhou Ruhong, Freed Karl F, Sosnick Tobin R

Abstract excerpt

Experimental and computational folding studies of Proteins L & G and NuG2 typically find that sequence differences determine which of the two hairpins is formed in the transition state ensemble (TSE). However, our recent work on Protein L finds that its TSE contains both hairpins, compelling a reassessment of the influence of sequence on the folding behavior of the other two homologs. We characterize the TSEs for...

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Identifiers

PMID: 26100906
DOI: 10.1073/pnas.1503613112
PMCID: PMC4500205

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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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