Exploring the conformational energy landscape of proteins
- 作者：Ulrich Nienhaus ; G. ; Mü ; ller ; Joachim D. ; McMahon ; Ben H. ; Frauenfelder ; Hans
- 关键词：Protein dynamics ; Conformational substates ; Energy landscape ; Myoglobin ; Infrared spectroscopy
- 刊名：Physica D
- 出版年：1997
- 期刊代码：55_01672789
- 类别：ph
- 出版时间：September 1, 1997
- 卷：107
- 期：2-4
- 页码：297-311
- 文件大小：1.12 M
摘要
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 hiearchy, 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 hiearchy contain a large number of statistical substates. Substate interconventions 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.