19F nuclear magnetic resonance studies of selectively fluorinated derivatives of G- and F-actin.

Abstract:

:G-Actin is a globular protein (Mr 42 300) known to have three cysteine residues that are at least partially exposed and chemically reactive (Cys-10, -284, and -374). When G-actin was reacted with 3-bromo-1,1,1-trifluoropropanone, three resolvable 19F resonances were observed in the 19F NMR spectrum. This fluorinated G-actin derivative remained fully polymerizable, and its 31P NMR spectrum was not significantly different from that of unmodified G-actin, indicating that the chemical modification did not denature the actin and the modified residues do not interfere with the extent of polymerization or the binding of adenosine 5'-triphosphate. One of the three 19F resonances was assigned to fluorinated Cys-374 on the basis of its selective reaction with N-ethylmaleimide. This resonance was dramatically broadened after polymerization of fluorinated G-actin, while the other two resonances were not markedly broadened or shifted. Thus, Cys-10 and -284 are not involved in or appreciably affected by the polymerization of G-actin, while the mobility of the 19F label at Cys-374 is markedly reduced.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Brauer M,Sykes BD

doi

10.1021/bi00356a050

subject

Has Abstract

pub_date

1986-04-22 00:00:00

pages

2187-91

issue

8

eissn

0006-2960

issn

1520-4995

journal_volume

25

pub_type

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