Exploring Protein Conformational Landscapes Using High-Pressure NMR.
Methods Enzymol
; 614: 293-320, 2019.
Article
in En
| MEDLINE
| ID: mdl-30611428
ABSTRACT
Protein conformational landscapes define their functional properties as well as their proteostasis. Hence, detailed mapping of these landscapes is necessary to understand and modulate protein conformation. The combination of high pressure and NMR provides a particularly powerful approach to characterizing protein conformational transitions. First, pressure, because its effects on protein structure arise from elimination of solvent excluded void volume, represents a more subtle perturbation than chemical denaturants, favoring the population of intermediates. Second, the residue-specific and multifaceted nature of NMR observables informs on many local structural properties of proteins, aiding in the characterization of intermediate and excited states.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Nuclear Magnetic Resonance, Biomolecular
/
Intracellular Signaling Peptides and Proteins
/
Connectin
Limits:
Humans
Language:
En
Journal:
Methods Enzymol
Year:
2019
Document type:
Article
Affiliation country: