Details

Autor(en) / Beteiligte

• Jain, Shefali
• Sekhar, Ashok

Titel

Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy

Ist Teil von

• Journal of Magnetic Resonance Open, 2022-06, Vol.10-11, p.100034-100034, Article 100034

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2022

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• •NMR is a tool that is well-suited for deciphering the molecular mechanisms.•Conformational selection and induced fit pathways can be distinguished by NMR.•Saturation transfer and relaxation dispersion can detect sparsely populated states.•DRD-CEST is a new method to differentiate between sequential and parallel pathways. How proteins switch between various ligand-free and ligand-bound structures has been a key biophysical question ever since the postulation of the Monod-Wyman-Changeux and Koshland-Nemethy-Filmer models over six decades ago. The ability of NMR spectroscopy to provide structural and kinetic information on biomolecular conformational exchange places it in a unique position as an analytical tool to interrogate the mechanisms of biological processes such as protein folding and biomolecular complex formation. In addition, recent methodological developments in the areas of saturation transfer and relaxation dispersion have expanded the scope of NMR for probing the mechanics of transitions in systems where one or more states constituting the exchange process are sparsely populated and 'invisible' in NMR spectra. In this review, we highlight some of the strategies available from NMR spectroscopy for examining the nature of multi-site conformational exchange, using five case studies that have employed NMR, either in isolation, or in conjunction with other biophysical tools. [Display omitted]