Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3 + groups of proteins at low temperature
Author:
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s10858-014-9854-y.pdf
Reference26 articles.
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2. Andre I, Linse S, Mulder FA (2007) Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: application to apo calmodulin. J Am Chem Soc 129:15805–15813
3. Blaum BS, Deakin JA, Johansson CM, Herbert AP, Barlow PN, Lyon M, Uhrín D (2010) Lysine and arginine side chains in glycosaminoglycan-protein complexes investigated by NMR, cross-linking, and mass spectrometry: a case study of the factor H-heparin interaction. J Am Chem Soc 132:6374–6381
4. Esadze A, Iwahara J (2014) Stopped-flow fluorescence kinetic study of protein sliding and intersegment transfer in the target DNA search process. J Mol Biol 426:230–244
5. Esadze A, Li DW, Wang T, Brüschweiler R, Iwahara J (2011) Dynamics of lysine side-chain amino groups in a protein studied by heteronuclear 1H-15N NMR spectroscopy. J Am Chem Soc 133:909–919
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