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Journal Abstract Search

1357 related items for PubMed ID: 25574774

  • 1. Enzyme dynamics from NMR spectroscopy.
    Palmer AG.
    Acc Chem Res; 2015 Feb 17; 48(2):457-65. PubMed ID: 25574774
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  • 2. Characterization of enzyme motions by solution NMR relaxation dispersion.
    Loria JP, Berlow RB, Watt ED.
    Acc Chem Res; 2008 Feb 17; 41(2):214-21. PubMed ID: 18281945
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  • 3. Conformational preferences underlying reduced activity of a thermophilic ribonuclease H.
    Stafford KA, Trbovic N, Butterwick JA, Abel R, Friesner RA, Palmer AG.
    J Mol Biol; 2015 Feb 27; 427(4):853-866. PubMed ID: 25550198
    [Abstract] [Full Text] [Related]

  • 4. Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation.
    Desamero R, Rozovsky S, Zhadin N, McDermott A, Callender R.
    Biochemistry; 2003 Mar 18; 42(10):2941-51. PubMed ID: 12627960
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  • 5. Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes.
    Butterwick JA, Loria JP, Astrof NS, Kroenke CD, Cole R, Rance M, Palmer AG.
    J Mol Biol; 2004 Jun 11; 339(4):855-71. PubMed ID: 15165855
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  • 9. Changes in protein dynamics of the DNA repair dioxygenase AlkB upon binding of Fe(2+) and 2-oxoglutarate.
    Bleijlevens B, Shivarattan T, van den Boom KS, de Haan A, van der Zwan G, Simpson PJ, Matthews SJ.
    Biochemistry; 2012 Apr 24; 51(16):3334-41. PubMed ID: 22443471
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  • 11. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
    Rozovsky S, Jogl G, Tong L, McDermott AE.
    J Mol Biol; 2001 Jun 29; 310(1):271-80. PubMed ID: 11419952
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  • 12. Quantitative analysis of conformational exchange contributions to 1H-15N multiple-quantum relaxation using field-dependent measurements. Time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant.
    Lundström P, Akke M.
    J Am Chem Soc; 2004 Jan 28; 126(3):928-35. PubMed ID: 14733570
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  • 13. Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase.
    McCallum SA, Hitchens TK, Torborg C, Rule GS.
    Biochemistry; 2000 Jun 27; 39(25):7343-56. PubMed ID: 10858281
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  • 14. Protein dynamics control the progression and efficiency of the catalytic reaction cycle of the Escherichia coli DNA-repair enzyme AlkB.
    Ergel B, Gill ML, Brown L, Yu B, Palmer AG, Hunt JF.
    J Biol Chem; 2014 Oct 24; 289(43):29584-601. PubMed ID: 25043760
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  • 17. 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 24; 41(3):442-51. PubMed ID: 18275162
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  • 18. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r).
    Otten R, Villali J, Kern D, Mulder FA.
    J Am Chem Soc; 2010 Dec 01; 132(47):17004-14. PubMed ID: 21058670
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  • 19. Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.
    Lisi GP, Loria JP.
    Prog Nucl Magn Reson Spectrosc; 2016 Feb 01; 92-93():1-17. PubMed ID: 26952190
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  • 20. Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
    Philippopoulos M, Lim C.
    Proteins; 1999 Jul 01; 36(1):87-110. PubMed ID: 10373009
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