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| Content Provider | PubMed Central |
|---|---|
| Author | Kinoshita, Masahiro |
| Copyright Year | 2009 |
| Abstract | We briefly review our studies on the folding/unfolding mechanisms of proteins. In biological self-assembly processes such as protein folding, the number of accessible translational configurations of water in the system increases greatly, leading to a large gain in the water entropy. The usual view looking at only the water in the close vicinity of the protein surface is capable of elucidating neither the large entropic gain upon apoplastocyanin folding, which has recently been found in a novel experimental study, nor the pressure and cold denaturation. With the emphasis on the translational entropy of water, we are presently constructing a reliable method for predicting the native structure of a protein from its amino-acid sequence. |
| Related Links | http://dx.doi.org/10.3390/ijms10031064 |
| Ending Page | 1080 |
| Page Count | 17 |
| Starting Page | 1064 |
| File Format | |
| ISSN | 14220067 |
| e-ISSN | 14220067 |
| Journal | International Journal of Molecular Sciences |
| Issue Number | 3 |
| Volume Number | 10 |
| Language | English |
| Publisher | Molecular Diversity Preservation International (MDPI) |
| Publisher Date | 2009-03-01 |
| Access Restriction | Open |
| Rights Holder | Molecular Diversity Preservation International (MDPI) |
| Subject Keyword | Physical and Theoretical Chemistry Inorganic Chemistry Organic Chemistry Spectroscopy Molecular Biology Catalysis Computer Science Applications Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Organic Chemistry Medicine Molecular Biology Physical and Theoretical Chemistry Catalysis Inorganic Chemistry Computer Science Applications |
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