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  Thermal coefficients of the methyl groups within ubiquitin.

Sabo, T. M., Bakhtiari, D., Walter, K. F. A., McFeeters, R., Giller, K., Becker, S., et al. (2012). Thermal coefficients of the methyl groups within ubiquitin. Protein Science, 21(4), 562-570. doi:10.1002/pro.2045.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-0BF3-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-2F0F-5
Genre: Journal Article

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Sabo, T. M.1, Author              
Bakhtiari, D.1, Author              
Walter, K. F. A.1, Author              
McFeeters, R., Author
Giller, K.1, Author              
Becker, S.1, Author              
Griesinger, C.1, Author              
Lee, D.1, Author              
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1Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: NMR; methyl group dynamics; cross-correlated relaxation; thermal coefficients; protein stability; ubiquitin
 Abstract: Physiological processes such as protein folding and molecular recognition are intricately linked to their dynamic signature, which is reflected in their thermal coefficient. In addition, the local conformational entropy is directly related to the degrees of freedom, which each residue possesses within its conformational space. Therefore, the temperature dependence of the local conformational entropy may provide insight into understanding how local dynamics may affect the stability of proteins. Here, we analyze the temperature dependence of internal methyl group dynamics derived from the cross-correlated relaxation between dipolar couplings of two CH bonds within ubiquitin. Spanning a temperature range from 275 to 308 K, internal methyl group dynamics tend to increase with increasing temperature, which translates to a general increase in local conformational entropy. With this data measured over multiple temperatures, the thermal coefficient of the methyl group order parameter, the characteristic thermal coefficient, and the local heat capacity were obtained. By analyzing the distribution of methyl group thermal coefficients within ubiquitin, we found that the N-terminal region has relatively high thermostability. These results indicate that methyl groups contribute quite appreciably to the total heat capacity of ubiquitin through the regulation of local conformational entropy.

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Language(s): eng - English
 Dates: 2012-03-022012-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pro.2045
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Title: Protein Science
Source Genre: Journal
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Pages: - Volume / Issue: 21 (4) Sequence Number: - Start / End Page: 562 - 570 Identifier: -