Photo-CIDNP NMR methods for studying protein folding.
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 o...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2004
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| _version_ | 1826304774714163200 |
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| author | Mok, K Hore, P |
| author_facet | Mok, K Hore, P |
| author_sort | Mok, K |
| collection | OXFORD |
| description | 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 (15)N-(1)H 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. |
| first_indexed | 2024-03-07T06:22:52Z |
| format | Journal article |
| id | oxford-uuid:f3441986-4a5b-489a-a01f-f6a8f40123f8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:22:52Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:f3441986-4a5b-489a-a01f-f6a8f40123f82022-03-27T12:10:49ZPhoto-CIDNP NMR methods for studying protein folding.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f3441986-4a5b-489a-a01f-f6a8f40123f8EnglishSymplectic Elements at Oxford2004Mok, KHore, PChemically 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 (15)N-(1)H 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. |
| spellingShingle | Mok, K Hore, P Photo-CIDNP NMR methods for studying protein folding. |
| title | Photo-CIDNP NMR methods for studying protein folding. |
| title_full | Photo-CIDNP NMR methods for studying protein folding. |
| title_fullStr | Photo-CIDNP NMR methods for studying protein folding. |
| title_full_unstemmed | Photo-CIDNP NMR methods for studying protein folding. |
| title_short | Photo-CIDNP NMR methods for studying protein folding. |
| title_sort | photo cidnp nmr methods for studying protein folding |
| work_keys_str_mv | AT mokk photocidnpnmrmethodsforstudyingproteinfolding AT horep photocidnpnmrmethodsforstudyingproteinfolding |