Relaxation dynamics in heme proteins

A protein molecule possesses many conformational substates that are likely arranged in a hierarchy consisting of a number of tiers. A hierarchical organization of conformational substates is expected to give rise to a multitude of nonequilibrium relaxation phenomena. If the temperature is lowered, transitions between substates of higher tiers are frozen out, and relaxation processes characteristic of lower tiers will dominate the observational time scale.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Physics

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Scholl, Reinhard Wilhelm

Contributors dc:contributor

• Frauenfelder, Hans

• Physics, Molecular
• Biophysics, General

Statement dc:rights

• Copyright 1991 Scholl, Reinhard Wilhelm

Language dc:language

eng

Identifier

AAI9210980
(UMI)AAI9210980

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20973