Role of the solvent in the dynamical transitions of proteins:The case of the lysozyme-water system
We study the dynamics of hydration water in the protein lysozyme in the temperature range 180 K < T < 360 K using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. By analyzing the thermal evolution of spectra of the OH-stretching vibration modes and the NMR self-...
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| Veröffentlicht in: | The Journal of chemical physics 2007-07, Vol.127 (4), p.045104-045104-6 |
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| container_end_page | 045104-6 |
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| container_issue | 4 |
| container_start_page | 045104 |
| container_title | The Journal of chemical physics |
| container_volume | 127 |
| creator | Mallamace, Francesco Chen, Sow-Hsin Broccio, Matteo Corsaro, Carmelo Crupi, Vincenza Majolino, Domenico Venuti, Valentina Baglioni, Piero Fratini, Emiliano Vannucci, Chiara Stanley, H. Eugene |
| description | We study the dynamics of hydration water in the protein lysozyme in the temperature range
180
K
<
T
<
360
K
using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. By analyzing the thermal evolution of spectra of the OH-stretching vibration modes and the NMR self-diffusion
(
D
S
)
and spin-lattice relaxation time
(
T
1
)
, we demonstrate the existence of two dynamical transitions in the protein hydration water. Below the first transition, at about
220
K
, the hydration water displays an unambiguous fragile-to-strong dynamic crossover, resulting in the loss of the protein conformational flexibility. Above the second transition, at about
346
K
, where the protein unfolds, the dynamics of the hydration water appears to be dominated by the non-hydrogen-bonded fraction of water molecules. |
| doi_str_mv | 10.1063/1.2757171 |
| format | Article |
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180
K
<
T
<
360
K
using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. By analyzing the thermal evolution of spectra of the OH-stretching vibration modes and the NMR self-diffusion
(
D
S
)
and spin-lattice relaxation time
(
T
1
)
, we demonstrate the existence of two dynamical transitions in the protein hydration water. Below the first transition, at about
220
K
, the hydration water displays an unambiguous fragile-to-strong dynamic crossover, resulting in the loss of the protein conformational flexibility. Above the second transition, at about
346
K
, where the protein unfolds, the dynamics of the hydration water appears to be dominated by the non-hydrogen-bonded fraction of water molecules.</description><identifier>ISSN: 0021-9606</identifier><identifier>EISSN: 1089-7690</identifier><identifier>DOI: 10.1063/1.2757171</identifier><identifier>PMID: 17672727</identifier><identifier>CODEN: JCPSA6</identifier><language>eng</language><publisher>United States: American Institute of Physics</publisher><subject>Computer Simulation ; Models, Chemical ; Models, Molecular ; Muramidase - chemistry ; Muramidase - ultrastructure ; Phase Transition ; Protein Conformation ; Protein Denaturation ; Protein Folding ; Solvents - chemistry ; Structure-Activity Relationship ; Water - chemistry</subject><ispartof>The Journal of chemical physics, 2007-07, Vol.127 (4), p.045104-045104-6</ispartof><rights>2007 American Institute of Physics</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-786f37009bffb5d20ab77ffd8804b471a01f5154d8a9d91e0788da2ba1f877e13</citedby><cites>FETCH-LOGICAL-c403t-786f37009bffb5d20ab77ffd8804b471a01f5154d8a9d91e0788da2ba1f877e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,794,1559,4512,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17672727$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mallamace, Francesco</creatorcontrib><creatorcontrib>Chen, Sow-Hsin</creatorcontrib><creatorcontrib>Broccio, Matteo</creatorcontrib><creatorcontrib>Corsaro, Carmelo</creatorcontrib><creatorcontrib>Crupi, Vincenza</creatorcontrib><creatorcontrib>Majolino, Domenico</creatorcontrib><creatorcontrib>Venuti, Valentina</creatorcontrib><creatorcontrib>Baglioni, Piero</creatorcontrib><creatorcontrib>Fratini, Emiliano</creatorcontrib><creatorcontrib>Vannucci, Chiara</creatorcontrib><creatorcontrib>Stanley, H. Eugene</creatorcontrib><title>Role of the solvent in the dynamical transitions of proteins:The case of the lysozyme-water system</title><title>The Journal of chemical physics</title><addtitle>J Chem Phys</addtitle><description>We study the dynamics of hydration water in the protein lysozyme in the temperature range
180
K
<
T
<
360
K
using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. By analyzing the thermal evolution of spectra of the OH-stretching vibration modes and the NMR self-diffusion
(
D
S
)
and spin-lattice relaxation time
(
T
1
)
, we demonstrate the existence of two dynamical transitions in the protein hydration water. Below the first transition, at about
220
K
, the hydration water displays an unambiguous fragile-to-strong dynamic crossover, resulting in the loss of the protein conformational flexibility. Above the second transition, at about
346
K
, where the protein unfolds, the dynamics of the hydration water appears to be dominated by the non-hydrogen-bonded fraction of water molecules.</description><subject>Computer Simulation</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - ultrastructure</subject><subject>Phase Transition</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Solvents - chemistry</subject><subject>Structure-Activity Relationship</subject><subject>Water - chemistry</subject><issn>0021-9606</issn><issn>1089-7690</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1Lw0AQQBdRbK0e_AOSk-AhdSZJsxvBgxS_oCBIPS-bZBdXkmzNbJX4601s0JPMYRh4PIbH2CnCHCGNL3Ee8QVHjntsiiCykKcZ7LMpQIRhlkI6YUdEbwCAPEoO2QR5yqN-pix_dpUOnAn8qw7IVR-68YFtfs6ya1RtC1UFvlUNWW9dQwO7aZ3XtqGrdU8Vin4FVUfuq6t1-Km8bgPqyOv6mB0YVZE-GfeMvdzdrpcP4erp_nF5swqLBGIfcpGamANkuTH5ooxA5ZwbUwoBSZ5wVIBmgYukFCorM9TAhShVlCs0gnON8Yyd77z9e-9bTV7WlgpdVarRbksyFYgZQNyDFzuwaB1Rq43ctLZWbScR5BBUohyD9uzZKN3mtS7_yLFgD1zvACqsV0Oi_21Da-mM7FPJsXX8DURyhg4</recordid><startdate>20070728</startdate><enddate>20070728</enddate><creator>Mallamace, Francesco</creator><creator>Chen, Sow-Hsin</creator><creator>Broccio, Matteo</creator><creator>Corsaro, Carmelo</creator><creator>Crupi, Vincenza</creator><creator>Majolino, Domenico</creator><creator>Venuti, Valentina</creator><creator>Baglioni, Piero</creator><creator>Fratini, Emiliano</creator><creator>Vannucci, Chiara</creator><creator>Stanley, H. Eugene</creator><general>American Institute of Physics</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>7X8</scope></search><sort><creationdate>20070728</creationdate><title>Role of the solvent in the dynamical transitions of proteins:The case of the lysozyme-water system</title><author>Mallamace, Francesco ; Chen, Sow-Hsin ; Broccio, Matteo ; Corsaro, Carmelo ; Crupi, Vincenza ; Majolino, Domenico ; Venuti, Valentina ; Baglioni, Piero ; Fratini, Emiliano ; Vannucci, Chiara ; Stanley, H. Eugene</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-786f37009bffb5d20ab77ffd8804b471a01f5154d8a9d91e0788da2ba1f877e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Computer Simulation</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - ultrastructure</topic><topic>Phase Transition</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Solvents - chemistry</topic><topic>Structure-Activity Relationship</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mallamace, Francesco</creatorcontrib><creatorcontrib>Chen, Sow-Hsin</creatorcontrib><creatorcontrib>Broccio, Matteo</creatorcontrib><creatorcontrib>Corsaro, Carmelo</creatorcontrib><creatorcontrib>Crupi, Vincenza</creatorcontrib><creatorcontrib>Majolino, Domenico</creatorcontrib><creatorcontrib>Venuti, Valentina</creatorcontrib><creatorcontrib>Baglioni, Piero</creatorcontrib><creatorcontrib>Fratini, Emiliano</creatorcontrib><creatorcontrib>Vannucci, Chiara</creatorcontrib><creatorcontrib>Stanley, H. Eugene</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of chemical physics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mallamace, Francesco</au><au>Chen, Sow-Hsin</au><au>Broccio, Matteo</au><au>Corsaro, Carmelo</au><au>Crupi, Vincenza</au><au>Majolino, Domenico</au><au>Venuti, Valentina</au><au>Baglioni, Piero</au><au>Fratini, Emiliano</au><au>Vannucci, Chiara</au><au>Stanley, H. Eugene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of the solvent in the dynamical transitions of proteins:The case of the lysozyme-water system</atitle><jtitle>The Journal of chemical physics</jtitle><addtitle>J Chem Phys</addtitle><date>2007-07-28</date><risdate>2007</risdate><volume>127</volume><issue>4</issue><spage>045104</spage><epage>045104-6</epage><pages>045104-045104-6</pages><issn>0021-9606</issn><eissn>1089-7690</eissn><coden>JCPSA6</coden><abstract>We study the dynamics of hydration water in the protein lysozyme in the temperature range
180
K
<
T
<
360
K
using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. By analyzing the thermal evolution of spectra of the OH-stretching vibration modes and the NMR self-diffusion
(
D
S
)
and spin-lattice relaxation time
(
T
1
)
, we demonstrate the existence of two dynamical transitions in the protein hydration water. Below the first transition, at about
220
K
, the hydration water displays an unambiguous fragile-to-strong dynamic crossover, resulting in the loss of the protein conformational flexibility. Above the second transition, at about
346
K
, where the protein unfolds, the dynamics of the hydration water appears to be dominated by the non-hydrogen-bonded fraction of water molecules.</abstract><cop>United States</cop><pub>American Institute of Physics</pub><pmid>17672727</pmid><doi>10.1063/1.2757171</doi><tpages>1</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9606 |
| ispartof | The Journal of chemical physics, 2007-07, Vol.127 (4), p.045104-045104-6 |
| issn | 0021-9606 1089-7690 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68119003 |
| source | MEDLINE; AIP Journals Complete; AIP Digital Archive |
| subjects | Computer Simulation Models, Chemical Models, Molecular Muramidase - chemistry Muramidase - ultrastructure Phase Transition Protein Conformation Protein Denaturation Protein Folding Solvents - chemistry Structure-Activity Relationship Water - chemistry |
| title | Role of the solvent in the dynamical transitions of proteins:The case of the lysozyme-water system |
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