Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 368

1.

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy.

Vallurupalli P, Hansen DF, Kay LE.

Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11766-71. doi: 10.1073/pnas.0804221105. Epub 2008 Aug 13.

2.

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
3.

Quantifying two-bond 1HN-13CO and one-bond 1H(alpha)-13C(alpha) dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy.

Hansen DF, Vallurupalli P, Kay LE.

J Am Chem Soc. 2008 Jul 2;130(26):8397-405. doi: 10.1021/ja801005n. Epub 2008 Jun 3.

PMID:
18528998
4.

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
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.

Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy.

Lundström P, Hansen DF, Vallurupalli P, Kay LE.

J Am Chem Soc. 2009 Feb 11;131(5):1915-26. doi: 10.1021/ja807796a.

PMID:
19152327
7.

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.

Hansen DF, Vallurupalli P, Kay LE.

J Am Chem Soc. 2009 Sep 9;131(35):12745-54. doi: 10.1021/ja903897e.

PMID:
19685870
8.
9.

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
10.

Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do?

Hansen DF, Vallurupalli P, Lundström P, Neudecker P, Kay LE.

J Am Chem Soc. 2008 Feb 27;130(8):2667-75. doi: 10.1021/ja078337p. Epub 2008 Feb 1.

PMID:
18237174
11.

Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.

Hansen DF, Neudecker P, Kay LE.

J Am Chem Soc. 2010 Jun 9;132(22):7589-91. doi: 10.1021/ja102090z.

PMID:
20465253
12.

Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy.

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

J Am Chem Soc. 2009 Aug 12;131(31):10832-3. doi: 10.1021/ja904315m.

PMID:
19606858
13.

Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples.

Lundström P, Hansen DF, Kay LE.

J Biomol NMR. 2008 Sep;42(1):35-47. doi: 10.1007/s10858-008-9260-4. Epub 2008 Sep 2.

PMID:
18762869
14.

Probing structure in invisible protein states with anisotropic NMR chemical shifts.

Vallurupalli P, Hansen DF, Kay LE.

J Am Chem Soc. 2008 Mar 5;130(9):2734-5. doi: 10.1021/ja710817g. Epub 2008 Feb 8.

PMID:
18257570
15.

Measurement of bond vector orientations in invisible excited states of proteins.

Vallurupalli P, Hansen DF, Stollar E, Meirovitch E, Kay LE.

Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18473-7. Epub 2007 Nov 15.

16.

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
17.

Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings.

Mohana-Borges R, Goto NK, Kroon GJ, Dyson HJ, Wright PE.

J Mol Biol. 2004 Jul 23;340(5):1131-42.

PMID:
15236972
18.

Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy.

Lundström P, Lin H, Kay LE.

J Biomol NMR. 2009 Jul;44(3):139-55. doi: 10.1007/s10858-009-9321-3. Epub 2009 May 16.

PMID:
19448976
19.

Studying "invisible" excited protein states in slow exchange with a major state conformation.

Vallurupalli P, Bouvignies G, Kay LE.

J Am Chem Soc. 2012 May 16;134(19):8148-61. doi: 10.1021/ja3001419. Epub 2012 May 3.

PMID:
22554188
20.

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.

Supplemental Content

Support Center