NMR spectroscopy brings invisible protein states into focus.
Molecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we descri...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2009
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| _version_ | 1826262176031047680 |
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| author | Baldwin, A Kay, L |
| author_facet | Baldwin, A Kay, L |
| author_sort | Baldwin, A |
| collection | OXFORD |
| description | Molecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we describe recent advances in NMR spectroscopy methods that enable studies of these otherwise invisible excited states at an atomic level and that help elucidate their important relation to function. We discuss a range of examples from molecular recognition, ligand binding, enzyme catalysis and protein folding that illustrate the role that motion plays in 'funneling' conformers along preferred pathways that facilitate their biological function. |
| first_indexed | 2024-03-06T19:32:15Z |
| format | Journal article |
| id | oxford-uuid:1dd964e3-6651-43c0-9498-7b3c6fcad0b0 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:32:15Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:1dd964e3-6651-43c0-9498-7b3c6fcad0b02022-03-26T11:13:12ZNMR spectroscopy brings invisible protein states into focus.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1dd964e3-6651-43c0-9498-7b3c6fcad0b0EnglishSymplectic Elements at Oxford2009Baldwin, AKay, LMolecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we describe recent advances in NMR spectroscopy methods that enable studies of these otherwise invisible excited states at an atomic level and that help elucidate their important relation to function. We discuss a range of examples from molecular recognition, ligand binding, enzyme catalysis and protein folding that illustrate the role that motion plays in 'funneling' conformers along preferred pathways that facilitate their biological function. |
| spellingShingle | Baldwin, A Kay, L NMR spectroscopy brings invisible protein states into focus. |
| title | NMR spectroscopy brings invisible protein states into focus. |
| title_full | NMR spectroscopy brings invisible protein states into focus. |
| title_fullStr | NMR spectroscopy brings invisible protein states into focus. |
| title_full_unstemmed | NMR spectroscopy brings invisible protein states into focus. |
| title_short | NMR spectroscopy brings invisible protein states into focus. |
| title_sort | nmr spectroscopy brings invisible protein states into focus |
| work_keys_str_mv | AT baldwina nmrspectroscopybringsinvisibleproteinstatesintofocus AT kayl nmrspectroscopybringsinvisibleproteinstatesintofocus |