ThaumatinV1, Main, Corpus, bibRecord, 000242

Protein dynamical transition at 110 K.

Identifieur interne : 000242 ( Main/Corpus ); précédent : 000241; suivant : 000243

Protein dynamical transition at 110 K.

Auteurs : Chae Un Kim ; Mark W. Tate ; Sol M. Gruner

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2011.

RBID : pubmed:22167801

English descriptors

KwdEn :
- Cold Temperature (MeSH), Crystallography, X-Ray (MeSH), Plant Proteins (chemistry), Pressure (MeSH), Protein Conformation (MeSH), Water (chemistry).
MESH :
- chemical , chemistry : Plant Proteins, Water.
- Cold Temperature, Crystallography, X-Ray, Pressure, Protein Conformation.

Abstract

Proteins are known to undergo a dynamical transition at around 200 K but the underlying mechanism, physical origin, and relationship to water are controversial. Here we report an observation of a protein dynamical transition as low as 110 K. This unexpected protein dynamical transition precisely correlated with the cryogenic phase transition of water from a high-density amorphous to a low-density amorphous state. The results suggest that the cryogenic protein dynamical transition might be directly related to the two liquid forms of water proposed at cryogenic temperatures.

DOI: 10.1073/pnas.1110840108
PubMed: 22167801
PubMed Central: PMC3248492

Links to Exploration step

pubmed:22167801

Le document en format XML

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<author><name sortKey="Kim, Chae Un" sort="Kim, Chae Un" uniqKey="Kim C" first="Chae Un" last="Kim">Chae Un Kim</name>
<affiliation><nlm:affiliation>Cornell High Energy Synchrotron Source, Laboratory of Atomic and Solid State Physics, and Department of Physics, Cornell University, Ithaca, NY 14853, USA. ck243@cornell.edu</nlm:affiliation>
</affiliation>
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<author><name sortKey="Tate, Mark W" sort="Tate, Mark W" uniqKey="Tate M" first="Mark W" last="Tate">Mark W. Tate</name>
</author>
<author><name sortKey="Gruner, Sol M" sort="Gruner, Sol M" uniqKey="Gruner S" first="Sol M" last="Gruner">Sol M. Gruner</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Protein dynamical transition at 110 K.</title>
<author><name sortKey="Kim, Chae Un" sort="Kim, Chae Un" uniqKey="Kim C" first="Chae Un" last="Kim">Chae Un Kim</name>
<affiliation><nlm:affiliation>Cornell High Energy Synchrotron Source, Laboratory of Atomic and Solid State Physics, and Department of Physics, Cornell University, Ithaca, NY 14853, USA. ck243@cornell.edu</nlm:affiliation>
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<author><name sortKey="Tate, Mark W" sort="Tate, Mark W" uniqKey="Tate M" first="Mark W" last="Tate">Mark W. Tate</name>
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<author><name sortKey="Gruner, Sol M" sort="Gruner, Sol M" uniqKey="Gruner S" first="Sol M" last="Gruner">Sol M. Gruner</name>
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<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
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<term>Crystallography, X-Ray (MeSH)</term>
<term>Plant Proteins (chemistry)</term>
<term>Pressure (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Water (chemistry)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term>
<term>Water</term>
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<front><div type="abstract" xml:lang="en">Proteins are known to undergo a dynamical transition at around 200 K but the underlying mechanism, physical origin, and relationship to water are controversial. Here we report an observation of a protein dynamical transition as low as 110 K. This unexpected protein dynamical transition precisely correlated with the cryogenic phase transition of water from a high-density amorphous to a low-density amorphous state. The results suggest that the cryogenic protein dynamical transition might be directly related to the two liquid forms of water proposed at cryogenic temperatures.</div>
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<Abstract><AbstractText>Proteins are known to undergo a dynamical transition at around 200 K but the underlying mechanism, physical origin, and relationship to water are controversial. Here we report an observation of a protein dynamical transition as low as 110 K. This unexpected protein dynamical transition precisely correlated with the cryogenic phase transition of water from a high-density amorphous to a low-density amorphous state. The results suggest that the cryogenic protein dynamical transition might be directly related to the two liquid forms of water proposed at cryogenic temperatures.</AbstractText>
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Protein dynamical transition at 110 K.

Protein dynamical transition at 110 K.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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