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Exploring the conformational energy landscape of proteins

Conference ·
OSTI ID:464177
 [1]; ;  [2]
  1. Univ. of Illinois, Urbana, IL (United States)
  2. Univ. of Illinois, Urbana, IL (United States); and others

Proteins possess a complex energy landscape with a large number of local minima called conformational substates that are arranged in a hierarchical fashion. Here we discuss experiments aimed at the elucidation of the energy landscape in carbonmonoxy myoglobin (MbCO). In the highest tier of the hierarchy, a few taxonomic substates exist. Because of their small number, these substates are accessible to detailed structural investigations. Spectroscopic experiments are discussed that elucidate the role of protonations of amino acid side chains in creating the substates. The lower tiers of the hierarchy contain a large number of statistical substates. Substate interconversions are observed in the entire temperature range from below 1 K up to the denaturation temperature, indicating a wide spectrum of energy barriers that separate the substates.

Research Organization:
Los Alamos National Lab., NM (United States)
Sponsoring Organization:
USDOE Office of Energy Research, Washington, DC (United States); National Insts. of Health, Bethesda, MD (United States)
DOE Contract Number:
W-7405-ENG-36
OSTI ID:
464177
Report Number(s):
LA-UR--97-503; CONF-970597--1; ON: DE97004792; CNN: Grant GM 18051
Country of Publication:
United States
Language:
English

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