Importance of translational entropy of water in biological self-assembly processes like protein folding
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 l...
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| Veröffentlicht in: | International journal of molecular sciences 2009-03, Vol.10 (3), p.1064-1080 |
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| creator | Kinoshita, Masahiro |
| description | 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. |
| doi_str_mv | 10.3390/ijms10031064 |
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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.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms10031064</identifier><identifier>PMID: 19399238</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Apoproteins - chemistry ; Apoproteins - metabolism ; Entropy ; Plastocyanin - chemistry ; Plastocyanin - metabolism ; Pressure ; Protein Denaturation ; Protein Folding ; Review ; Temperature ; Water - chemistry</subject><ispartof>International journal of molecular sciences, 2009-03, Vol.10 (3), p.1064-1080</ispartof><rights>Copyright MDPI AG 2009</rights><rights>2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. 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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.</description><subject>Apoproteins - chemistry</subject><subject>Apoproteins - metabolism</subject><subject>Entropy</subject><subject>Plastocyanin - chemistry</subject><subject>Plastocyanin - metabolism</subject><subject>Pressure</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Review</subject><subject>Temperature</subject><subject>Water - chemistry</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc9r2zAUx8VYWdJst52HYYde6u5Jsq3oUiihvyDQy3YWsvycKZMtV3Ja8t9XJmHNdpK-fD98ee99CflK4YpzCT_stosUgFOoig9kTgvGcoBKfDz5z8h5jFsAxlkpP5EZlVxKxpdzsnnsBh9G3RvMfJuNQffR6dH6XrsM-zH4YT8Zr3rEkNk-q613fmNNsiO6NtcxYle7fTYEbzCJmDn7Byc5YuJb7xrbbz6Ts1a7iF-O74L8urv9uXrI10_3j6ubdW4KIcbcVNVSNsVScFoXLWsAapBoAI02QpQVNFVtKCsEB4ZCp_2xFHVb0qSXZSv5glwfcodd3WFjphW0U0OwnQ575bVV_zq9_a02_kWxSjCgU8DFMSD45x3GUXU2GnRO9-h3UQnOQfKK00R-_4_c-l1Id4uKlunOshSUJeryQJngYwzY_p2FgpoKVKcFJvzb6fzv8LEx_gYkW5jB</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Kinoshita, Masahiro</creator><general>MDPI AG</general><general>Molecular Diversity Preservation International (MDPI)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090301</creationdate><title>Importance of translational entropy of water in biological self-assembly processes like protein folding</title><author>Kinoshita, Masahiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-c6689d48731b4f2d00b09ec0ecac77560d6bc1247302e7a390e57bf5130285f93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Apoproteins - 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| identifier | ISSN: 1422-0067 |
| ispartof | International journal of molecular sciences, 2009-03, Vol.10 (3), p.1064-1080 |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Apoproteins - chemistry Apoproteins - metabolism Entropy Plastocyanin - chemistry Plastocyanin - metabolism Pressure Protein Denaturation Protein Folding Review Temperature Water - chemistry |
| title | Importance of translational entropy of water in biological self-assembly processes like protein folding |
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