Related ArticlesTemperature 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 temperature dependence of overall rotational diffusion and local backbone motion. Correlation between the order parameter of the N-H vector, SNH2, and that of the carbonyl carbon, S2C', was investigated. The effective S2C' was estimated from the direct fit of the experimental relaxation rates and from the slope of 2R2-R1 vs. B2 using Lipari-Szabo formalism. The average SNH2 decreased by 5.9%, while the average S2C' decreased by 4.6% from 15 to 47 degrees C. At the extreme low and high temperatures the difference in the temperature dependence of the order parameters vanishes. At the intermediate temperatures they do not change by the same amount but they follow the same trend. On the same peptide plane along the protein sequence, S2C' and SNH2 are highly correlated. The results suggest that fast local motion experienced at the site of the N-H vector and carbonyl nucleus is more complicated than previously thought and it cannot be easily described by one single type of motion in a broad range of temperature.
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] A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR
A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations.
Related Articles A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations.
J Biomol NMR. 2005 Feb;31(2):87-95
Authors: Ko?mi?ski W, Zhukov I, Pecul M, Sadlej J
A new pulse sequence exploiting double- and zero-quantum evolution of two-spin 15N-13C' coherence is proposed for the accurate measurements of 2J(N(i),C alpha(i-1)) coupling...
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11-24-2010 11:14 PM
[NMR paper] Temperature dependence of NMR order parameters and protein dynamics.
Temperature dependence of NMR order parameters and protein dynamics.
Related Articles Temperature dependence of NMR order parameters and protein dynamics.
J Am Chem Soc. 2003 Sep 17;125(37):11158-9
Authors: Massi F, Palmer AG
The helical subdomain, HP36, of the F-actin-binding headpiece domain of chicken villin, is the smallest naturally occurring polypeptide that folds to a thermostable compact structure. Unconstrained molecular dynamics simulations and constrained molecular dynamics simulations using umbrella sampling are used to study the...
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11-24-2010 09:16 PM
[NMR paper] Temperature-dependence of protein hydrogen bond properties as studied by high-resolut
Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR.
Related Articles Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR.
J Mol Biol. 2002 Apr 12;317(5):739-52
Authors: Cordier F, Grzesiek S
The temperature-dependence of a large number of NMR parameters describing hydrogen bond properties in the protein ubiquitin was followed over a range from 5 to 65 degrees C. The parameters comprise hydrogen bond (H-bond) scalar couplings, h3JNC', chemical shifts, amide...
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11-24-2010 08:49 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
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100508u/aop/images/medium/bi-2010-00508u_0005.gifBiochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
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08-31-2010 10:50 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...
Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR
Linear Mode
