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Article

Characterization of the molten globule conformation of V26A ubiquitin by far-UV circular dichroic spectroscopy and amide hydrogen/deuterium exchange.

BMB reports - 31 Jan 2008

Park Soon-Ho

Abstract excerpt

The molten globular conformation of V26A ubiquitin (valine to alanine mutation at residue 26) was studied by nuclear magnetic resonance spectroscopy in conjunction with amide hydrogen/deuterium exchange. Most of the amide protons that are involved in the native secondary structures were observed to be protected in the molten globule state with the protection factors from 1.2 to 6.7. These protection factors are...

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Identifiers

PMID: 18304448
DOI: 10.5483/bmbrep.2008.41.1.035

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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