Dynamics of blue copper proteins

Studies of small molecules binding to heme proteins have yielded a large amount of information about protein dynamics and conformational substates (CS) in proteins. However, heme proteins are very similar in their active site structures, and relatively little work exists on non-heme proteins which is directly comparable to the heme protein experiments. We have therefore studied the binding of NO to three blue copper proteins, a class of proteins which lack a heme group and have a different structural motif from that of heme proteins.

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

• Ehrenstein, David Henry

Contributors dc:contributor

• Frauenfelder, Hans

• Biophysics, General
• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1995 Ehrenstein, David Henry

Language dc:language

eng

Identifier

AAI9522106
(UMI)AAI9522106

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22900