This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/25638
Description
Title
Heme protein structure and ligand binding
Author(s)
Nordlund, Thomas Michael
Issue Date
1977
Doctoral Committee Chair(s)
Frauenfelder, Hans
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
heme proteins
heme protein structure
ligand binding
carbon monoxide binding
hemoglobin
Language
en
Abstract
Binding of carbon monoxide to a variety of heme proteins is a multistep process and can be described by a sequence of activation barriers. In the separated alpha and beta chains of hemoglobin three
barriers are found which are sensitive to the structural differences between the two chains. The barriers in the beta chain change when two cysteine amino acids are modified with a mercury compound. Three processes are also observed in CO binding to cytochrome P4S0 and rates depend strongly upon the presence of the enzyme's substrate, camphor. Comparisons among these and other heme proteins and compounds show that protein structure can influence any of the activation barriers.
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.
