| Protein elasticity determined by pressure tuning of the tyrosine residue of ubiquitin. | |
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MedLine Citation:
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PMID: 17824766 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We determined the isotropic, isothermal compressibility of ubiquitin by pressure tuning spectral holes burnt into the red edge of the absorption spectrum of the single tyrosine residue. The pressure shift is perfectly linear with burn frequency. From these data, a compressibility of 0.086 GPa(-1) in the local environment of the tyrosine residue could be determined. This value fits nicely into the range known for proteins. Although the elastic behavior at low temperatures does not show any unusual features, the pressure tuning behavior at room temperature is quite surprising: the pressure-induced spectral shift is close to zero, even up to very high pressure levels of 0.88 GPa, well beyond the denaturation point. The reason for this behavior is attributed to equally strong blue as well as red spectral pressure shifts resulting in an average pressure-induced solvent shift that is close to zero. |
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Authors:
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Mark M Somoza; Johannes Wiedersich; Josef Friedrich |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Journal of chemical physics Volume: 127 ISSN: 0021-9606 ISO Abbreviation: J Chem Phys Publication Date: 2007 Sep |
Date Detail:
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Created Date: 2007-09-10 Completed Date: 2007-11-13 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0375360 Medline TA: J Chem Phys Country: United States |
Other Details:
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Languages: eng Pagination: 095102 Citation Subset: IM |
Affiliation:
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Physik-Department E14 and Lehrstuhl für Physik Weihenstephan, Technische Universität München, 85350 Freising, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Computer Simulation Elasticity Models, Chemical* Models, Molecular* Pressure Protein Conformation Stress, Mechanical Tyrosine / chemistry* Ubiquitin / chemistry*, ultrastructure* |
| Chemical | |
Reg. No./Substance:
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0/Ubiquitin; 55520-40-6/Tyrosine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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