| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5384770 | Chemical Physics Letters | 2011 | 6 Pages |
Abstract
⺠MD simulations of psychrophilic and mesophilic α-amylases were carried out. ⺠We calculated protein conformational entropy changes upon substrate bindings. ⺠The entropy changes were decomposed into contributions of individual amino acids. ⺠Differences of entropy changes are found to be attributed to the insertion residues. ⺠Difference in the entropy change well explains the temperature dependences.
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Authors
Takahiro Kosugi, Shigehiko Hayashi,