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- W2024193039 endingPage "87" @default.
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- W2024193039 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 experiments permit the observation of changes in the accessibility of specific residues during the folding process. CIDNP pulse-labeling gives information on the accessibility of residues in partially structured proteins (e.g., molten globule states) whose NMR spectra are broad and poorly resolved. Heteronuclear two-dimensional 15N–1H CIDNP techniques allow identification of surface-accessible residues with improved resolution and sensitivity. These methods offer residue-specific structural and kinetic information on transient folding intermediates and other partially folded states of proteins that are not readily available from more routine NMR techniques." @default.
- W2024193039 created "2016-06-24" @default.
- W2024193039 creator A5070141094 @default.
- W2024193039 date "2004-09-01" @default.
- W2024193039 modified "2023-10-07" @default.
- W2024193039 title "Photo-CIDNP NMR methods for studying protein folding" @default.
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- W2024193039 doi "https://doi.org/10.1016/j.ymeth.2004.03.006" @default.
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