The time-zero HSQC method improves the linear free energy relationship of a polypeptide chain through the accurate measurement of residue-specific equilibrium constants-Reference-Cited by-同舟云学术

The time-zero HSQC method improves the linear free energy relationship of a polypeptide chain through the accurate measurement of residue-specific equilibrium constants

Published:2022-06 Issue:3 Volume:76 Page:87-94
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Hayashi Seiichiro^ORCID,Kohda Daisuke^ORCID

Funder

Japan Society for the Promotion of Science

Mitsubishi Foundation

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

https://link.springer.com/content/pdf/10.1007/s10858-022-00396-y.pdf

Reference17 articles.

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3. Farrow NA, Zhang O, Forman-Kay JD, Kay LE (1995) Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer. Biochemistry 34:868–878. https://doi.org/10.1021/bi00003a021

4. Farrow NA, Zhang O, Forman-Kay JD, Kay LE (1994) A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium. J Biomol NMR 4:727–734. https://doi.org/10.1007/BF00404280

5. Fersht AR, Matouschek A, Serrano L (1992) The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol 224:771–782. https://doi.org/10.1016/0022-2836(92)90561-W

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