NMR spectroscopy brings invisible protein states into focus.

Journal article

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 ra...

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Authors: Baldwin, A; Kay, L

• Publication status: Published
• Journal: Nature chemical biology
• Volume: 5
• Issue: 11
• Pages: 808-814
• Publication date: 2009-11-01
• DOI: 10.1038/nchembio.238
• EISSN: 1552-4469
• ISSN: 1552-4450
• Language: English
• Keywords: Cytochromes c; Peptides; Magnetic Resonance Spectroscopy; Thermodynamics; Ubiquitin; Protein Folding; Kinetics; Proteins; Catalysis; Models, Molecular; Enzymes; Protein Conformation; Photochemistry