ATP-induced conformational transition of denatured proteins.

Abstract:

:Although the conformational change occurring in proteins upon ATP binding is important in many biological reactions, the mechanism by which ATP binding induces the conformational change is unknown. We found that ATP induces acid-unfolded (pH 2) ferricytochrome c or apomyoglobin to adopt a compact structure with a significant amount of alpha-helix and increased hydrophobicity. A very similar conformational transition was observed at neutral pH for an amphiphilic model polypeptide. The effectiveness of various adenine nucleotides in inducing the conformational transition was found to be proportional to their phosphate group contents, i.e., adenosine tetraphosphate greater than ATP greater than ADP greater than AMP. These results should be important when considering the mechanism of the ATP-induced conformational change in proteins during various biological reactions.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Goto Y,Okamura N,Aimoto S

doi

10.1093/oxfordjournals.jbchem.a123451

keywords:

subject

Has Abstract

pub_date

1991-05-01 00:00:00

pages

746-50

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

109

pub_type

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