Journal
CHEMICAL PHYSICS LETTERS
Volume 474, Issue 1-3, Pages 190-194Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cplett.2009.04.025
Keywords
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [20118004]
- Grand Challenges in Next-Generation Integrated Nanoscience, MEXT, Japan
- Grants-in-Aid for Scientific Research [20118004] Funding Source: KAKEN
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We have recently shown that the water entropy is the key quantity in elucidating the folding/unfolding mechanisms for proteins. Here we consider thermal denaturation. The water-entropy gain upon the transition from the random-coil state to the native structure is calculated for some representative proteins by employing the angle-dependent integral equation theory combined with the multipolar water model and the morphometric approach. It is found that the water-entropy gain at 25 degrees C divided by the number of residues is a good measure of the thermal stability. A protein with a larger value of this measure tends to have a higher denaturation temperature. (C) 2009 Elsevier B. V. All rights reserved.
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