Slow Motions in the HydrophobicCore of Chicken Villin Headpiece Subdomain and Their Contributionsto Configurational Entropy and Heat Capacity from Solid-State DeuteronNMR Measurements
Slow Motions in the HydrophobicCore of Chicken Villin Headpiece Subdomain and Their Contributionsto Configurational Entropy and Heat Capacity from Solid-State DeuteronNMR Measurements
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Abstract X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down...
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08-13-2011 02:47 AM
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
J Biomol NMR. 2011 Aug 9;
Authors: Linden AH, Franks WT, Akbey U, Lange S, van Rossum BJ, Oschkinat H
X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100*K. Protein dynamics are poorly understood...
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08-10-2011 12:30 PM
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] Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain fold
Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
Related Articles Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
J Am Chem Soc. 2003 May 21;125(20):6032-3
Authors: Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP
There is considerable interest in small proteins that fold very rapidly. These proteins have become attractive targets for both theoretical and computational studies. The...
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11-24-2010 09:01 PM
[NMR paper] Identification of slow motions in the reduced recombinant high-potential iron sulfur
Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
Related Articles Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
J Biomol NMR. 1998 Aug;12(2):307-18
Authors: Banci L, Felli IC, Koulougliotis D
Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been...
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11-17-2010 11:15 PM
[NMR paper] Contributions to protein entropy and heat capacity from bond vector motions measured
Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation.
J Mol Biol. 1997 Oct 10;272(5):790-804
Authors: Yang D, Mok YK, Forman-Kay JD, Farrow NA, Kay LE
The backbone dynamics of both folded and unfolded states of staphylococcal nuclease (SNase) and the N-terminal...
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08-22-2010 05:08 PM
[NMR paper] NMR evidence for slow collective motions in cyanometmyoglobin.
NMR evidence for slow collective motions in cyanometmyoglobin.
Related Articles NMR evidence for slow collective motions in cyanometmyoglobin.
Nat Struct Biol. 1997 Apr;4(4):292-7
Authors: Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH
Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic...
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08-22-2010 03:31 PM
[NMR paper] NMR evidence for slow collective motions in cyanometmyoglobin.
NMR evidence for slow collective motions in cyanometmyoglobin.
Related Articles NMR evidence for slow collective motions in cyanometmyoglobin.
Nat Struct Biol. 1997 Apr;4(4):292-7
Authors: Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH
Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic...
Slow Motions in the HydrophobicCore of Chicken Villin Headpiece Subdomain and Their Contributionsto Configurational Entropy and Heat Capacity from Solid-State DeuteronNMR Measurements
Linear Mode
