The temperature dependence of the hydrogen exchange in the SH3 domain of α-spectrin

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Title: The temperature dependence of the hydrogen exchange in the SH3 domain of α-spectrin
Authors: Sadqi, M.1, Casares, S.1, López-Mayorga, O.1, Conejero-Lara, F. conejero@ugr.es
Source: FEBS Letters. Sep2002, Vol. 527 Issue 1-3, p86. 5p.
Subjects: Homology (Biology), Amides
Abstract: The amide hydrogen–deuterium exchange (HX) in the Src homology region 3 (SH3) domain of α-spectrin has been measured by nuclear magnetic resonance as a function of temperature between 8 and 46°C. The analysis of the temperature dependence of HX from a statistical thermodynamic point of view has allowed us to estimate the enthalpies and entropies of the conformational processes leading to HX. The results indicate that under native conditions the domain undergoes a wide variety of conformational fluctuations, ranging from local motions, mainly located in loops, turns and chain ends and involving only low enthalpy and entropy, to extensive structural disruptions affecting its core and involving enthalpies and entropies that come fairly close to those observed during global unfolding. [Copyright &y& Elsevier]
Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: The temperature dependence of the hydrogen exchange in the SH3 domain of α-spectrin
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  Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Sep2002, Vol. 527 Issue 1-3, p86. 5p.
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– Name: Abstract
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  Data: The amide hydrogen–deuterium exchange (HX) in the Src homology region 3 (SH3) domain of α-spectrin has been measured by nuclear magnetic resonance as a function of temperature between 8 and 46°C. The analysis of the temperature dependence of HX from a statistical thermodynamic point of view has allowed us to estimate the enthalpies and entropies of the conformational processes leading to HX. The results indicate that under native conditions the domain undergoes a wide variety of conformational fluctuations, ranging from local motions, mainly located in loops, turns and chain ends and involving only low enthalpy and entropy, to extensive structural disruptions affecting its core and involving enthalpies and entropies that come fairly close to those observed during global unfolding. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
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  Group: Ab
  Data: <i>Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/S0014-5793(02)03172-1
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        Text: English
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      – TitleFull: The temperature dependence of the hydrogen exchange in the SH3 domain of α-spectrin
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