The folding process of apomyoglobin.

Abstract:

:Apomyoglobin (apoMb) folds through at least two partially folded forms that are detected both as transient intermediates during folding/unfolding kinetics or as stable intermediates at equilibrium. Here, I summarize the results of recent kinetic studies, which combined with detailed characterizations of equilibrium forms of the protein, provide a very detailed picture of apoMb folding process. The data are consistent with a linear U<->Ia<->Ib<->N model where compaction and structure are progressively acquired.

journal_name

Protein Pept Lett

authors

Jamin M

doi

10.2174/0929866053587174

subject

Has Abstract

pub_date

2005-04-01 00:00:00

pages

229-34

issue

3

eissn

0929-8665

issn

1875-5305

journal_volume

12

pub_type

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