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
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Abstract We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By...
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05-24-2011 10:00 AM
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
J Biomol NMR. 2011 Mar 18;
Authors: Bouvignies G, Vallurupalli P, Cordes MH, Hansen DF, Kay LE
A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated 'invisible' protein states that exchange...
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03-23-2011 05:41 PM
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy
Abstract A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated â??invisibleâ?? protein states that exchange with a â??visibleâ?? ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold...
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03-22-2011 07:32 PM
[NMR paper] Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR
Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation.
Related Articles Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation.
J Magn Reson. 2005 May;174(1):43-53
Authors: Chang SL, Tjandra N
The NMR spin-lattice relaxation rate (R1) and the rotating-frame spin-lattice relaxation rate (R1rho) of amide 15N and carbonyl 13C (13C') of the uniformly 13C- and 15N-labeled ubiquitin were measured at different temperatures and field strengths to investigate the...
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11-25-2010 08:21 PM
Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of t
Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of the Tryptophan Repressor Protein (TrpR): Comparison with the 15N NMR Relaxation Profiles of Wild-Type and A77V Mutant Apo-TrpR Repressors
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08-31-2010 10:50 PM
[NMR paper] The hydration of proteins in solutions by self-diffusion coefficients. NMR study.
The hydration of proteins in solutions by self-diffusion coefficients. NMR study.
Related Articles The hydration of proteins in solutions by self-diffusion coefficients. NMR study.
Biochim Biophys Acta. 1996 Apr 17;1289(3):312-4
Authors: Baranowska HM, Olszewski KJ
The hydration of the globular (lysozyme, albumin) and fibrillar (fibrinogen) proteins in solution has been determined from the measurements of the self-diffusion coefficient by NMR pulsed gradient method. It has been concluded that the concentration dependencies of the...
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08-22-2010 02:27 PM
[NMR paper] Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
Related Articles Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
J Biomol NMR. 1991 May;1(1):65-70
Authors: Akasaka K, Naito A, Nakatani H
The kinetic process of folding of bovine pancreatic ribonuclease A in a 2H2O environment at pH 1.2 was examined by a recently developed temperature-jump NMR method (Akasaka et al., (1990) Rev. Sci. Instrum. 61, 66-68). Upon temperature-jump down from 45 degrees C to 29 degrees C, which was attained within 6 s,...
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08-21-2010 11:16 PM
Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of t
Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of the tryptophan repressor protein (TrpR): comparison with the 15N NMR relaxation profiles of wild type and A77V mutant apo-TrpR repressors.
Related Articles Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of the tryptophan repressor protein (TrpR): comparison with the 15N NMR relaxation profiles of wild type and A77V mutant apo-TrpR repressors.
Biochemistry. 2010 Aug 18;
Authors: Goel A, Tripet BP, Tyler RC, Nebert LD, Copie V
...
Amide temperature coefficients in the protein G B1 domain
Linear Mode
