Motions in myoglobin

When the structure of myoglobin was first revealed by x-ray crystallography, it was discovered that there was no clear evidence of a pathway for ligands to enter the protein to bind at the heme iron. Motions within the protein are necessary for the protein to function. Pressure release and flash photolysis experiments help characterize some of these protein motions.

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

• Johnson, Jeffrey Bruce

Contributors dc:contributor

• Frauenfelder, Hans

• Physics, General

Statement dc:rights

• Copyright 1991 Johnson, Jeffrey Bruce

Language dc:language

eng

Identifier

AAI9136629
(UMI)AAI9136629

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20300