Journal article

Photo-CIDNP NMR methods for studying protein folding.

Abstract:: Chemically induced dynamic nuclear polarization (CIDNP) is a nuclear magnetic resonance phenomenon that can be used to probe the solvent-accessibility of tryptophan, tyrosine, and histidine residues in proteins by means of laser-induced photochemical reactions, resulting in significant enhancement of NMR signals. CIDNP offers good sensitivity as a surface probe of protein structure and is particularly powerful in time-resolved NMR measurements. Real-time, rapid-injection protein refolding exp...
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Publication status:: Published

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APA Style

Mok, K., & Hore, P. (2004). Photo-CIDNP NMR methods for studying protein folding. Methods (San Diego, Calif.), 34(1), 75–87.

MLA Style

Mok, K., and P. Hore. “Photo-CIDNP NMR Methods for Studying Protein Folding.” Methods (San Diego, Calif.), vol. 34, no. 1, 2004, pp. 75–87.

Chicago Style

Mok, K, and P Hore. 2004. “Photo-CIDNP NMR Methods for Studying Protein Folding.” Methods (San Diego, Calif.) 34 (1): 75–87.
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Publisher copy:: 10.1016/j.ymeth.2004.03.006

Authors

+ Mok, K More by this author

Role:

Author

+ Hore, P More by this author

Institution:

University of Oxford

Division:

MPLS

Department:

Chemistry

Sub department:

Physical & Theoretical Chem

Role:

Author

Bibliographic Details

Journal:: Methods (San Diego, Calif.) More from this journal
Volume:: 34
Issue:: 1
Pages:: 75-87
Publication date:: 2004-09-01
DOI:: 10.1016/j.ymeth.2004.03.006
EISSN:: 1095-9130
ISSN:: 1046-2023

Item Description

Language:: English
Keywords:: Magnetic Resonance Spectroscopy

Protein Folding

Solutions

Tryptophan

Histidine

Tyrosine
Pubs id:: pubs:32803
UUID:: uuid:f3441986-4a5b-489a-a01f-f6a8f40123f8
Local pid:: pubs:32803
Source identifiers:: 32803
Deposit date:: 2012-12-19

Terms of use

Copyright date:: 2004

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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