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Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.

We use mass spectrometry in conjunction with hydrogen-deuterium exchange and NMR to characterize the conformational dynamics of the 62-residue IgG binding domain of protein L under conditions in which the native state is marginally stable. Mass spectra of protein L after short incubations in D2O rev...

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Detalhes bibliográficos
Main Authors: Yi, Q., Baker, D.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1996
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143434/
https://ncbi.nlm.nih.gov/pubmed/8762137
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