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Items: 1 to 20 of 97

1.

The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements.

Li P, Martins IR, Rosen MK.

J Biomol NMR. 2011 Sep;51(1-2):57-70. doi: 10.1007/s10858-011-9541-1. Epub 2011 Sep 27.

2.

Thermodynamic and structural properties of r(ACC) as revealed by ultraviolet electronic absorption, circular dichroism, 1H-NMR spectroscopy and Monte Carlo simulations.

Bouchemal-Chibani N, Lebrun A, Hervé du Penhoat C, Ghomi M, Laigle A, Derouet C, Turpin PY.

J Biomol Struct Dyn. 1994 Dec;12(3):695-724.

PMID:
7727067
4.

Faithful estimation of dynamics parameters from CPMG relaxation dispersion measurements.

Kovrigin EL, Kempf JG, Grey MJ, Loria JP.

J Magn Reson. 2006 May;180(1):93-104. Epub 2006 Feb 3.

PMID:
16458551
5.

Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states.

Hansen DF, Vallurupalli P, Kay LE.

J Biomol NMR. 2008 Jul;41(3):113-20. doi: 10.1007/s10858-008-9251-5. Epub 2008 Jun 24.

PMID:
18574698
6.

Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes.

Hansen AL, Lundström P, Velyvis A, Kay LE.

J Am Chem Soc. 2012 Feb 15;134(6):3178-89. doi: 10.1021/ja210711v. Epub 2012 Feb 2.

PMID:
22300166
7.

CPMG relaxation dispersion.

Ishima R.

Methods Mol Biol. 2014;1084:29-49. doi: 10.1007/978-1-62703-658-0_2.

PMID:
24061914
8.

Using NMR chemical shifts as structural restraints in molecular dynamics simulations of proteins.

Robustelli P, Kohlhoff K, Cavalli A, Vendruscolo M.

Structure. 2010 Aug 11;18(8):923-33. doi: 10.1016/j.str.2010.04.016.

9.

Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding.

Korzhnev DM, Kay LE.

Acc Chem Res. 2008 Mar;41(3):442-51. doi: 10.1021/ar700189y. Epub 2008 Feb 15. Review.

PMID:
18275162
10.
11.

Accuracy and precision of protein-ligand interaction kinetics determined from chemical shift titrations.

Markin CJ, Spyracopoulos L.

J Biomol NMR. 2012 Dec;54(4):355-76. doi: 10.1007/s10858-012-9678-6. Epub 2012 Oct 21.

PMID:
23086713
13.

Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected ¹³C CPMG relaxation dispersion.

Weininger U, Respondek M, Akke M.

J Biomol NMR. 2012 Sep;54(1):9-14. doi: 10.1007/s10858-012-9656-z. Epub 2012 Jul 26.

14.

Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy.

Baldwin AJ, Hansen DF, Vallurupalli P, Kay LE.

J Am Chem Soc. 2009 Aug 26;131(33):11939-48. doi: 10.1021/ja903896p.

PMID:
19627152
15.

Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.

Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE.

Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15717-22. Epub 2007 Sep 26.

16.

Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods.

Auer R, Hansen DF, Neudecker P, Korzhnev DM, Muhandiram DR, Konrat R, Kay LE.

J Biomol NMR. 2010 Mar;46(3):205-16. doi: 10.1007/s10858-009-9394-z. Epub 2009 Dec 22.

PMID:
20033258
17.

Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.

Hansen DF, Neudecker P, Vallurupalli P, Mulder FA, Kay LE.

J Am Chem Soc. 2010 Jan 13;132(1):42-3. doi: 10.1021/ja909294n.

PMID:
20000605
18.

Binding mechanism of an SH3 domain studied by NMR and ITC.

Demers JP, Mittermaier A.

J Am Chem Soc. 2009 Apr 1;131(12):4355-67. doi: 10.1021/ja808255d.

PMID:
19267471
19.

Advances in solid-state relaxation methodology for probing site-specific protein dynamics.

Lewandowski JR.

Acc Chem Res. 2013 Sep 17;46(9):2018-27. doi: 10.1021/ar300334g. Epub 2013 Apr 26. Review.

PMID:
23621579
20.
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