Motions in myoglobin
type: CreativeWork
description: 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.
abstract: 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.
author: Johnson, Jeffrey Bruce
language: eng
keywords: Physics, General
date published: 2011-05-07T12:35:18Z
date modified: 2026-07-22T22:25:15Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/20300