Amide temperature coefficients in the protein G B1 domain
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...
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11-14-2011 08:45 AM
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain
Abstract Temperature-dependence of protein dynamics can provide information on details of the free energy landscape by probing the characteristics of the potential responsible for the fluctuations. We have investigated the temperature-dependence of picosecond to nanosecond backbone dynamics at carbonyl carbon sites in chicken villin headpiece subdomain protein using a combination of three NMR relaxation rates: 13Câ?² longitudinal rate, and two cross-correlated rates involving dipolar and...
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03-20-2011 07:14 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
[NMR paper] Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mu
Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.
Related Articles Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.
Biochemistry. 2002 Oct 8;41(40):11954-62
Authors: Tyler R, Pelczer I, Carey J, Copié V
L75F-TrpR is a temperature-sensitive mutant of the tryptophan repressor protein of Escherichia coli in which surface-exposed residue leucine 75 in the DNA binding domain is replaced with...
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11-24-2010 08:58 PM
[NMR paper] Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Biochemistry. 1996 Apr 16;35(15):4867-77
Authors: MacKay JP, Shaw GL, King GF
The backbone dynamics of the coiled-coil leucine zipper domain of c-Jun have been studied using proton-detected two-dimensional 1H-15N NMR spectroscopy. Longitudinal (T1) and transverse (T2) 15N relaxation times,...
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08-22-2010 02:27 PM
[NMR paper] Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA meth
Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA methylphosphotriester repair domain of Escherichia coli Ada using NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA methylphosphotriester repair domain of Escherichia coli Ada using NMR.
Biochemistry. 1996 Jul 23;35(29):9335-48
Authors: Habazettl J, Myers LC, Yuan F, Verdine GL, Wagner G
The 10kDa amino-terminal fragment of...
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08-22-2010 02:20 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
...
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08-21-2010 01:02 AM
Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin
Abstract We perform a detailed comparison of fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal domain (DHP) and its S74E mutant (DHPS74E). Carbonyl dynamics is probed via auto-correlated longitudinal rates and transverse Câ?²/Câ?²-Cα CSA/dipolar and Câ?²/Câ?²â??N CSA/dipolar cross-correlated rates, while 15N data are taken from a previous study. Resulting values of effective order parameters and internal correlation times support the conclusion that Câ?² relaxation reports on a different subset of fast motions compared to those...
Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of t
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