Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.
Identifieur interne : 000294 ( Main/Exploration ); précédent : 000293; suivant : 000295Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.
Auteurs : Matthew Warkentin [États-Unis] ; Robert E. ThorneSource :
- Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2010.
Descripteurs français
- KwdFr :
- Conformation des protéines (effets des radiations), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Modèles chimiques (MeSH), Plantes (MeSH), Protéines végétales (composition chimique), Radiotolérance (MeSH), Température (MeSH), Transition de phase (effets des radiations), Verre (composition chimique).
- MESH :
- composition chimique : Protéines végétales, Verre.
- effets des radiations : Conformation des protéines, Transition de phase.
- Cristallisation, Cristallographie aux rayons X, Modèles chimiques, Plantes, Radiotolérance, Température.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plant Proteins.
- chemistry : Glass.
- radiation effects : Phase Transition, Protein Conformation.
- Crystallization, Crystallography, X-Ray, Models, Chemical, Plants, Radiation Tolerance, Temperature.
Abstract
The temperature-dependence of radiation damage to thaumatin crystals between T = 300 and 100 K is reported. The amount of damage for a given dose decreases sharply as the temperature decreases from 300 to 220 K and then decreases more gradually on further cooling below the protein-solvent glass transition. Two regimes of temperature-activated behavior were observed. At temperatures above ∼200 K the activation energy of 18.0 kJ mol(-1) indicates that radiation damage is dominated by diffusive motions in the protein and solvent. At temperatures below ∼200 K the activation energy is only 1.00 kJ mol(-1), which is of the order of the thermal energy. Similar activation energies describe the temperature-dependence of radiation damage to a variety of solvent-free small-molecule organic crystals over the temperature range T = 300-80 K. It is suggested that radiation damage in this regime is vibrationally assisted and that the freezing-out of amino-acid scale vibrations contributes to the very weak temperature-dependence of radiation damage below ∼80 K. Analysis using the radiation-damage model of Blake and Phillips [Blake & Phillips (1962), Biological Effects of Ionizing Radiation at the Molecular Level, pp. 183-191] indicates that large-scale conformational and molecular motions are frozen out below T = 200 K but become increasingly prevalent and make an increasing contribution to damage at higher temperatures. Possible alternative mechanisms for radiation damage involving the formation of hydrogen-gas bubbles are discussed and discounted. These results have implications for mechanistic studies of proteins and for studies of the protein glass transition. They also suggest that data collection at T ≃ 220 K may provide a viable alternative for structure determination when cooling-induced disorder at T = 100 is excessive.
DOI: 10.1107/S0907444910035523
PubMed: 20944242
PubMed Central: PMC2954455
Affiliations:
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Thorne</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20944242</idno><idno type="pmid">20944242</idno><idno type="doi">10.1107/S0907444910035523</idno><idno type="pmc">PMC2954455</idno><idno type="wicri:Area/Main/Corpus">000275</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000275</idno><idno type="wicri:Area/Main/Curation">000275</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000275</idno><idno type="wicri:Area/Main/Exploration">000275</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.</title><author><name sortKey="Warkentin, Matthew" sort="Warkentin, Matthew" uniqKey="Warkentin M" first="Matthew" last="Warkentin">Matthew Warkentin</name><affiliation wicri:level="4"><nlm:affiliation>Physics Department, Cornell University, Ithaca, New York, USA. maw64@cornell.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Physics Department, Cornell University, Ithaca, New York</wicri:regionArea><placeName><region type="state">État de New York</region><settlement type="city">Ithaca (New York)</settlement></placeName><orgName type="university">Université Cornell</orgName></affiliation></author><author><name sortKey="Thorne, Robert E" sort="Thorne, Robert E" uniqKey="Thorne R" first="Robert E" last="Thorne">Robert E. Thorne</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="eISSN">1399-0047</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Glass (chemistry)</term><term>Models, Chemical (MeSH)</term><term>Phase Transition (radiation effects)</term><term>Plant Proteins (chemistry)</term><term>Plants (MeSH)</term><term>Protein Conformation (radiation effects)</term><term>Radiation Tolerance (MeSH)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (effets des radiations)</term><term>Cristallisation (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Modèles chimiques (MeSH)</term><term>Plantes (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Radiotolérance (MeSH)</term><term>Température (MeSH)</term><term>Transition de phase (effets des radiations)</term><term>Verre (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Glass</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines végétales</term><term>Verre</term></keywords><keywords scheme="MESH" qualifier="effets des radiations" xml:lang="fr"><term>Conformation des protéines</term><term>Transition de phase</term></keywords><keywords scheme="MESH" qualifier="radiation effects" xml:lang="en"><term>Phase Transition</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Models, Chemical</term><term>Plants</term><term>Radiation Tolerance</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Modèles chimiques</term><term>Plantes</term><term>Radiotolérance</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The temperature-dependence of radiation damage to thaumatin crystals between T = 300 and 100 K is reported. The amount of damage for a given dose decreases sharply as the temperature decreases from 300 to 220 K and then decreases more gradually on further cooling below the protein-solvent glass transition. Two regimes of temperature-activated behavior were observed. At temperatures above ∼200 K the activation energy of 18.0 kJ mol(-1) indicates that radiation damage is dominated by diffusive motions in the protein and solvent. At temperatures below ∼200 K the activation energy is only 1.00 kJ mol(-1), which is of the order of the thermal energy. Similar activation energies describe the temperature-dependence of radiation damage to a variety of solvent-free small-molecule organic crystals over the temperature range T = 300-80 K. It is suggested that radiation damage in this regime is vibrationally assisted and that the freezing-out of amino-acid scale vibrations contributes to the very weak temperature-dependence of radiation damage below ∼80 K. Analysis using the radiation-damage model of Blake and Phillips [Blake & Phillips (1962), Biological Effects of Ionizing Radiation at the Molecular Level, pp. 183-191] indicates that large-scale conformational and molecular motions are frozen out below T = 200 K but become increasingly prevalent and make an increasing contribution to damage at higher temperatures. Possible alternative mechanisms for radiation damage involving the formation of hydrogen-gas bubbles are discussed and discounted. These results have implications for mechanistic studies of proteins and for studies of the protein glass transition. They also suggest that data collection at T ≃ 220 K may provide a viable alternative for structure determination when cooling-induced disorder at T = 100 is excessive.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20944242</PMID><DateCompleted><Year>2011</Year><Month>05</Month><Day>17</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-0047</ISSN><JournalIssue CitedMedium="Internet"><Volume>66</Volume><Issue>Pt 10</Issue><PubDate><Year>2010</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.</ArticleTitle><Pagination><MedlinePgn>1092-100</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S0907444910035523</ELocationID><Abstract><AbstractText>The temperature-dependence of radiation damage to thaumatin crystals between T = 300 and 100 K is reported. The amount of damage for a given dose decreases sharply as the temperature decreases from 300 to 220 K and then decreases more gradually on further cooling below the protein-solvent glass transition. Two regimes of temperature-activated behavior were observed. At temperatures above ∼200 K the activation energy of 18.0 kJ mol(-1) indicates that radiation damage is dominated by diffusive motions in the protein and solvent. At temperatures below ∼200 K the activation energy is only 1.00 kJ mol(-1), which is of the order of the thermal energy. Similar activation energies describe the temperature-dependence of radiation damage to a variety of solvent-free small-molecule organic crystals over the temperature range T = 300-80 K. It is suggested that radiation damage in this regime is vibrationally assisted and that the freezing-out of amino-acid scale vibrations contributes to the very weak temperature-dependence of radiation damage below ∼80 K. Analysis using the radiation-damage model of Blake and Phillips [Blake & Phillips (1962), Biological Effects of Ionizing Radiation at the Molecular Level, pp. 183-191] indicates that large-scale conformational and molecular motions are frozen out below T = 200 K but become increasingly prevalent and make an increasing contribution to damage at higher temperatures. Possible alternative mechanisms for radiation damage involving the formation of hydrogen-gas bubbles are discussed and discounted. These results have implications for mechanistic studies of proteins and for studies of the protein glass transition. They also suggest that data collection at T ≃ 220 K may provide a viable alternative for structure determination when cooling-induced disorder at T = 100 is excessive.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Warkentin</LastName><ForeName>Matthew</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Physics Department, Cornell University, Ithaca, New York, USA. maw64@cornell.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thorne</LastName><ForeName>Robert E</ForeName><Initials>RE</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>DMR0225180</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P41 RR001646</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM065981</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM065981-05 A1</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>09</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005898" MajorTopicYN="N">Glass</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044367" MajorTopicYN="Y">Phase Transition</DescriptorName><QualifierName UI="Q000528" MajorTopicYN="N">radiation effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" 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York</li></region><settlement><li>Ithaca (New York)</li></settlement><orgName><li>Université Cornell</li></orgName></list><tree><noCountry><name sortKey="Thorne, Robert E" sort="Thorne, Robert E" uniqKey="Thorne R" first="Robert E" last="Thorne">Robert E. Thorne</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Warkentin, Matthew" sort="Warkentin, Matthew" uniqKey="Warkentin M" first="Matthew" last="Warkentin">Matthew Warkentin</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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