The Behavior of the Hydrophobic Effect under Pressure and Protein Denaturation
It is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of t...
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| Veröffentlicht in: | Biophysical journal 2010-04, Vol.98 (8), p.1626-1631 |
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| creator | Grigera, J. Raúl McCarthy, Andres N. |
| description | It is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of the effect of high pressure on globular proteins, such as lysozyme and apomyoglobin, we have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic effect that is known to be the main driving force in protein folding. |
| doi_str_mv | 10.1016/j.bpj.2009.12.4298 |
| format | Article |
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All rights reserved.</rights><rights>Copyright Biophysical Society Apr 21, 2010</rights><rights>2010 by the Biophysical Society.. 2010 Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c579t-e4b49d53de487c8564a62d72f8268a938316c1efd310229e696a140f19becfcb3</citedby><cites>FETCH-LOGICAL-c579t-e4b49d53de487c8564a62d72f8268a938316c1efd310229e696a140f19becfcb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856145/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349509061505$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3536,27903,27904,53769,53771,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20409483$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grigera, J. Raúl</creatorcontrib><creatorcontrib>McCarthy, Andres N.</creatorcontrib><title>The Behavior of the Hydrophobic Effect under Pressure and Protein Denaturation</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>It is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of the effect of high pressure on globular proteins, such as lysozyme and apomyoglobin, we have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic effect that is known to be the main driving force in protein folding.</description><subject>Analogies</subject><subject>Animals</subject><subject>Apoproteins - chemistry</subject><subject>Apoproteins - metabolism</subject><subject>Constraining</subject><subject>Denaturation</subject><subject>Dynamical systems</subject><subject>Folding</subject><subject>Hydrogen Bonding</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Models, Molecular</subject><subject>Molecular dynamics</subject><subject>Molecular Dynamics Simulation</subject><subject>Molecular structure</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobin - metabolism</subject><subject>Pressure</subject><subject>Protein</subject><subject>Protein Denaturation</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Simulation</subject><subject>Solvents</subject><subject>Sperm Whale</subject><subject>Surface Properties</subject><subject>Temperature</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEUx4Modlv9BzzI4MXTjPk9ExCh1mqFoh7qOWSSFzfDbrImMwv9782ybVEPegqPfN43L--D0AuCO4KJfDN1427qKMaqI7TjVA2P0IoITluMB_kYrTDGsmVciRN0WsqEMaECk6fohGKOFR_YCn25WUPzHtZmH1Jukm_mWl_dupx26zQG21x6D3ZuluggN98ylLJkaEx0tUgzhNh8gGjmJZs5pPgMPfFmU-D53XmGvn-8vLm4aq-_fvp8cX7dWtGruQU-cuUEc8CH3g5CciOp66kfqByMYgMj0hLwjhFMqQKppCEce6JGsN6O7Ay9O-bulnELzkKcs9noXQ5bk291MkH_eRPDWv9Ie03rY4SLGvD6LiCnnwuUWW9DsbDZmAhpKboXrBeE1R39l2RMcsmoquSrv8gpLTnWPWhKhFRckUMcPUI2p1Iy-IehCdYHrXrSVas-aNWE6oPW2vTy9-8-tNx7rMDbIwB16fsAWRcbIFpwIVd92qXwr_xf6EizEQ</recordid><startdate>20100421</startdate><enddate>20100421</enddate><creator>Grigera, J. 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Raúl ; McCarthy, Andres N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c579t-e4b49d53de487c8564a62d72f8268a938316c1efd310229e696a140f19becfcb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Analogies</topic><topic>Animals</topic><topic>Apoproteins - chemistry</topic><topic>Apoproteins - metabolism</topic><topic>Constraining</topic><topic>Denaturation</topic><topic>Dynamical systems</topic><topic>Folding</topic><topic>Hydrogen Bonding</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Models, Molecular</topic><topic>Molecular dynamics</topic><topic>Molecular Dynamics Simulation</topic><topic>Molecular structure</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobin - metabolism</topic><topic>Pressure</topic><topic>Protein</topic><topic>Protein Denaturation</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>Simulation</topic><topic>Solvents</topic><topic>Sperm Whale</topic><topic>Surface Properties</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grigera, J. 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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Analogies Animals Apoproteins - chemistry Apoproteins - metabolism Constraining Denaturation Dynamical systems Folding Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Models, Molecular Molecular dynamics Molecular Dynamics Simulation Molecular structure Myoglobin - chemistry Myoglobin - metabolism Pressure Protein Protein Denaturation Protein folding Proteins Simulation Solvents Sperm Whale Surface Properties Temperature |
| title | The Behavior of the Hydrophobic Effect under Pressure and Protein Denaturation |
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