Direct observation of fast protein folding: Distinct nanosecond and microsecond events in the folding of apomyoglobin

The rapid refolding dynamics of horse apomyoglobin are followed by a new temperature-jump fluorescence technique on a nanosecond to 0.5 millisecond time scale in vitro. Collapse to a compact state is complete in under 20 microseconds under strongly-nativizing conditions. The intrinsic tryptophan fluorescence (residue 14 in the A alpha helix) serves as a local probe of the A-helix and the disposition of the H alpha helix. Methionine (residue 131 in the H-helix) quenching of tryptophan fluorescence at the interface of the A- and H-helices in the compact or native-like structure is exploited to observe directly collapse from a cold denatured state to a molten globule or compact, native-like state. Refolding is characterized by distinct nanosecond and microsecond phenomena (250 nanoseconds and 3.5 microseconds).

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

1996

Author dc:creator

• Ballew, Richard Martin

Contributors dc:contributor

• Martin Gruebele

• Chemistry, Physical
• Biophysics, General

Statement dc:rights

• Copyright 1996 Ballew, Richard Martin

Language dc:language

eng

Identifier

9780591197365
AAI9712195
(UMI)AAI9712195

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/19174