Related ArticlesContributions 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 SH3 domain from drk (drkN SH3) are studied at two different temperatures. A simple method for obtaining order parameters, describing the amplitudes of motion of bond vectors, from NMR relaxation measurements of both folded and unfolded proteins is presented and the data obtained for 15N-NH bond vectors in both the SNase and drkN SH3 systems analyzed with this approach. Using a recently developed theory relating the amplitude of bond vector motions to conformational entropy, the entropy change between the folded and unfolded forms of SNase is calculated on a per residue basis. It is noteworthy that the region of the molecule with the smallest entropy change includes those residues showing native-like structure in the unfolded form of the molecule, as established by NOE-based experiments. Order parameters of backbone 15N-NH bond vectors show significantly larger changes with temperature in the unfolded states of both proteins relative to the corresponding folded forms. The differential temperature dependence is interpreted in terms of differences in the heat capacities of folded and unfolded polypeptide chains. The contribution to the heat capacity of the unfolded chain from rapid 15N-NH bond vector motions is calculated and compared with estimates of the heat capacity of the backbone unit, -CHCONH-, obtained from calorimetric data. Methyl dynamics measured at 14 and 30 degrees C establish that the amplitudes of side-chain motions in the folded SH3 domain are more sensitive to changes in temperature than the backbone dynamics, suggesting that over this temperature range side-chain ps to ns time-scale motions contribute more to the heat capacity than backbone motions for this protein.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
J Am Chem Soc. 2011 Apr 4;
Authors: Ryabov Y, Schwieters CD, Clore GM
(15)N R(2)/R(1) relaxation data contain information on molecular shape and size as well as on bond vector orientations relative to...
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Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Yaroslav Ryabov, Charles D. Schwieters and G. Marius Clore
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201020c/aop/images/medium/ja-2011-01020c_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201020c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/3J1IyCLkQMQ
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[NMR paper] What contributions to protein side-chain dynamics are probed by NMR experiments? A mo
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
Related Articles What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
J Mol Biol. 2005 May 27;349(1):185-203
Authors: Best RB, Clarke J, Karplus M
Molecular dynamics simulations of the structurally homologous proteins TNfn3 and FNfn10 have been used to investigate the contributions to side-chain dynamics measured by NMR relaxation experiments. The...
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11-24-2010 11:14 PM
[NMR paper] Contributions to conformational entropy arising from bond vector fluctuations measure
Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
J Mol Biol. 1996 Oct 25;263(2):369-82
Authors: Yang D, Kay LE
The relation between order parameters derived from NMR...
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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...
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08-21-2010 11:12 PM
[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...
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08-21-2010 11:12 PM
De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media
De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media
Ke Ruan, Kathryn B. Briggman and Joel R. Tolman
Journal of Biomolecular NMR; 2008; 41(2) pp 61 - 76
Abstract:
The straightforward interpretation of solution state residual dipolar couplings (RDCs) in terms of internuclear vector orientations generally requires prior knowledge of the alignment tensor, which in turn is normally estimated using a structural model. We have developed a protocol which allows the requirement for prior structural knowledge to...
Contributions to protein entropy and heat capacity from bond vector motions measured
Linear Mode
