The Relation among Thermodynamic Stability, Folding Dynamics, and Designability

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概要

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• We examined the relation among thermodynamic stability, folding rates, and designability at lattice proteins. We found no clear correlations among these three conditions. This implies that sequences having highly designable structure as native state do not necessarily satisfy both high thermodynamic stability and fast folding property. This conclusion may apply to natural proteins belonging to the same superfamily or superfold.

• 理論物理学刊行会の論文
• 2000-04-28

著者

• Matsuzaki K

  Institute For Materials Research Tohoku University

• Kikuchi M

  Tohoku Univ. Sendai Jpn

• Kikuchi Masae

  The Research Institute For Iron Steel And Other Metals Tohoku University

• AKUTSU Yasuhiro

  Institute of Physics, College of general Education University of Tokyo

• Akutsu Yasuhiro

  Department Of Physics Faculty Of Science Osaka University

• Chikenji George

  Department Of Computational Science And Engineering Nagoya University Graduate School Of Engineering

• Chikenji George

  Department Of Physics Graduate School Of Science Osaka University

• Kikuchi Macoto

  Department Of Physice Graduate School Of Science Osaka University

• Kikuchi Macoto

  Department Of Physics Graduate School Of Science Osaka University

• TATSUMI Rie

  Department of Physics, Graduate School of Science, Osaka University

• Tatsumi Rie

  Department Of Physics Graduate School Of Science Osaka University

• Moroishi Keiji

  Institute For Materials Research

• AKUTSU Yasuhiro

  Institute of Physics, College of Arts and Sciences University of Tokyo

• CHIKENJI George

  Department of Physics, Osaka University

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