TY - JOUR
T1 - Theoretical analysis on thermal stability of a protein focused on the water entropy
AU - Amano, Ken ichi
AU - Yoshidome, Takashi
AU - Harano, Yuichi
AU - Oda, Koji
AU - Kinoshita, Masahiro
N1 - Funding Information:
The development of our computer program for the morphometric approach was made possible by the collaboration with Roland Roth. We thank Annalisa Pastore for useful information on the native structures of the three frataxin orthologues. This work was supported by Grants-in-Aid for Scientific Research on Innovative Areas (No. 20118004) from the Ministry of Education, Culture, Sports, Science and Technology of Japan and by the Grand Challenges in Next-Generation Integrated Nanoscience, MEXT, Japan.
PY - 2009/5/25
Y1 - 2009/5/25
N2 - 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 °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.
AB - 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 °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.
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U2 - 10.1016/j.cplett.2009.04.025
DO - 10.1016/j.cplett.2009.04.025
M3 - Article
AN - SCOPUS:65549086981
SN - 0009-2614
VL - 474
SP - 190
EP - 194
JO - Chemical Physics Letters
JF - Chemical Physics Letters
IS - 1-3
ER -