| Pressure-induced Structural and Hydration Changes of Proteins in Aqueous Solutions. | |
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MedLine Citation:
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PMID: 22076342 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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The effects of elevated hydrostatic pressure on four representative proteins, lysozyme, human serum albumin, ubiquitin and RNase A, were investigated by using Fourier transform infrared (FTIR) spectroscopy, by principal component analysis (PCA) and by moving-window two-dimensional (MW2D) correlation analysis. In addition, we revealed the pressure-induced changes of secondary structure elements using curve fitting. With pressure increase, the amide I band shifted to lower wavenumbers, with a transition at 200 MPa, which was indicative of hydration enhancement. Moreover, the pressure-induced behavior of pure water was studied, similar transition pressure was observed with protein in aqueous solution, suggesting that structure change of water around 200 MPa caused a hydration enhancement of protein. Under pressure higher than 200 MPa, the structural changes of the four proteins were obviously different except for the common features shifting to lower wavenumbers with pressure, basically due to the distinct structural differences among them. |
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Authors:
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Min Zhang; Yuqing Wu |
Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Analytical sciences : the international journal of the Japan Society for Analytical Chemistry Volume: 27 ISSN: 1348-2246 ISO Abbreviation: Anal Sci Publication Date: 2011 |
Date Detail:
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Created Date: 2011-11-14 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8511078 Medline TA: Anal Sci Country: Japan |
Other Details:
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Languages: eng Pagination: 1139 Citation Subset: IM |
Affiliation:
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State Key Laboratory for Supramolecular Structure and Materials, Jilin University. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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