Amide temperature coefficients in the protein G B1 domain
Abstract Temperature coefficients have been measured for backbone amide 1H and 15N nuclei in the B1 domain of protein G (GB1), using temperatures in the range 283â??313 K, and pH values from 2.0 to 9.0. Many nuclei display pH-dependent coefficients, which were fitted to one or two pKa values. 1H coefficients showed the expected behaviour, in that hydrogen-bonded amides have less negative values, but for those amides involved in strong hydrogen bonds in regular secondary structure there is a negative correlation between strength of hydrogen bond and size of temperature coefficient. The best correlation to temperature coefficient is with secondary shift, indicative of a very approximately uniform thermal expansion. The largest pH-dependent changes in coefficient are for amides in loops adjacent to sidechain hydrogen bonds rather than the amides involved directly in hydrogen bonds, indicating that the biggest determinant of the temperature coefficient is temperature-dependent loss of structure, not hydrogen bonding. Amide 15N coefficients have no clear relationship with structure.
- Content Type Journal Article
- Category Article
- Pages 1-8
- DOI 10.1007/s10858-011-9583-4
- Authors
- Jennifer H. Tomlinson, Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN UK
- Mike P. Williamson, Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN UK
Source: Journal of Biomolecular NMR