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PMID: 1540692 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Determination of rate distributions from kinetic experiments.

Biophysical journal ·Vol. 61 ·No. 1 ·1992-01-00 ·Pages 235-45

Steinbach PJ, Chu K, Frauenfelder H, Johnson JB, Lamb DC, Nienhaus GU, Sauke TB, Young RD

Abstract

Rate processes in proteins are often not adequately described by simple exponential kinetics. Instead of modeling the kinetics in the time domain, it can be advantageous to perform a numerical inversion leading to a rate distribution function f(lambda). The features observed in f(lambda) (number, positions, and shapes of peaks) can then be interpreted. We discuss different numerical techniques for obtaining rate distribution functions, with special emphasis on the maximum entropy method. Examples are given for the application of these techniques to flash photolysis data of heme proteins.

MeSH Terms
Carbon Monoxide/blood Hemoglobins, Abnormal/metabolism Humans Kinetics Macromolecular Substances Mathematics Photolysis Protein Binding Proteins/metabolism Thermodynamics
Chemicals
Hemoglobins, Abnormal Macromolecular Substances Proteins Carbon Monoxide hemoglobin Zurich
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Steinbach P J
Department of Physics, University of Illinois, Urbana-Champaign 61801.
Chu K
Frauenfelder H
Johnson J B
Lamb D C
Nienhaus G U
Sauke T B
Young R D
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1016/S0006-3495(92)81830-1
Published
1992-01-00
Pages
235-45
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1260237
Subset
IM
Grants
NIGMS NIH HHS · GM-18051 · United States
NIGMS NIH HHS · GM-32455 · United States
External Links
PubMed source DOI: 10.1016/S0006-3495(92)81830-1 PMC Full Text View journal details
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