pH dependence of the hydrogen exchange in the SH3 domain of α-spectrin
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| Title: | pH dependence of the hydrogen exchange in the SH3 domain of α-spectrin |
|---|---|
| Authors: | Sadqi, M.1, Casares, S.1, López-Mayorga, O.1, Martınez, J.C.1, Conejero-Lara, F. conejero@ugr.es |
| Source: | FEBS Letters. Mar2002, Vol. 514 Issue 2/3, p295. 5p. |
| Subjects: | Spectrin, Nuclear magnetic resonance |
| Abstract: | Using nuclear magnetic resonance we have measured the hydrogen exchange (HX) in the Src homology region 3 (SH3) domain of α-spectrin as a function of pH*. At very acidic pH* values the exchange of most residues appears to occur via global unfolding, although several residues show abnormally large Gibbs energies of exchange, suggesting the presence of some residual structure in the unfolded state. At higher pH* HX occurs mainly via local or partial unfoldings. We have been able to characterize the coupling between the electrostatic interactions in this domain and the conformational fluctuations occurring under native conditions by analyzing the dependence upon pH* of the Gibbs energy of exchange. The SH3 domain seems to be composed of a central core, which requires large structural disruptions to become exposed to the solvent, surrounded by smaller subdomains, which fluctuate independently. [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.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: pH dependence of the hydrogen exchange in the SH3 domain of α-spectrin – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Sadqi%2C+M%2E%22">Sadqi, M.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Casares%2C+S%2E%22">Casares, S.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22López-Mayorga%2C+O%2E%22">López-Mayorga, O.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Martınez%2C+J%2EC%2E%22">Martınez, J.C.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Conejero-Lara%2C+F%2E%22">Conejero-Lara, F.</searchLink><i> conejero@ugr.es</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Mar2002, Vol. 514 Issue 2/3, p295. 5p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Spectrin%22">Spectrin</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+magnetic+resonance%22">Nuclear magnetic resonance</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Using nuclear magnetic resonance we have measured the hydrogen exchange (HX) in the Src homology region 3 (SH3) domain of α-spectrin as a function of pH*. At very acidic pH* values the exchange of most residues appears to occur via global unfolding, although several residues show abnormally large Gibbs energies of exchange, suggesting the presence of some residual structure in the unfolded state. At higher pH* HX occurs mainly via local or partial unfoldings. We have been able to characterize the coupling between the electrostatic interactions in this domain and the conformational fluctuations occurring under native conditions by analyzing the dependence upon pH* of the Gibbs energy of exchange. The SH3 domain seems to be composed of a central core, which requires large structural disruptions to become exposed to the solvent, surrounded by smaller subdomains, which fluctuate independently. [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: 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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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/S0014-5793(02)02385-2 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 5 StartPage: 295 Subjects: – SubjectFull: Spectrin Type: general – SubjectFull: Nuclear magnetic resonance Type: general Titles: – TitleFull: pH dependence of the hydrogen exchange in the SH3 domain of α-spectrin Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Sadqi, M. – PersonEntity: Name: NameFull: Casares, S. – PersonEntity: Name: NameFull: López-Mayorga, O. – PersonEntity: Name: NameFull: Martınez, J.C. – PersonEntity: Name: NameFull: Conejero-Lara, F. IsPartOfRelationships: – BibEntity: Dates: – D: 13 M: 03 Text: Mar2002 Type: published Y: 2002 Identifiers: – Type: issn-print Value: 00145793 Numbering: – Type: volume Value: 514 – Type: issue Value: 2/3 Titles: – TitleFull: FEBS Letters Type: main |
| ResultId | 1 |
