University of Illinois at Urbana-Champaign
Structural heterogeneity and conformational relaxation in heme proteins
Abstract
dc:descriptionThe influence of cooling rate upon the structural heterogeneity of sperm whale myoglobin solutions at cryogenic temperatures was studied. Sample cooling rates were varied by almost four orders of magnitude. FTIR spectra of the CO stretch frequency region reveal that the population of the A states is highly sensitive to the glass transition temperature T$\sb{\rm g}$ of the solvent, which is in turn sensitive to the cooling rate. The structural heterogeneity within each substate was assessed by temperature-derivative spectroscopy (TDS); no significant changes of barrier distributions were found. We conclude that cooling rate plays a negligible role in the structural heterogeneity of protein solutions, and that conformational substates are an intrinsic part of protein systems.
Degree
thesis:*- 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 and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Chu, Kelvin
- Contributors dc:contributor
-
- Nienhaus, Uli
Subjects
dc:subject × 3Rights
dc:rights- Statement dc:rights
-
- Copyright 1995 Chu, Kelvin
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
-
AAI9624317
(UMI)AAI9624317 - OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/21974