Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.
Molecules
; 25(23)2020 Nov 26.
Article
in En
| MEDLINE
| ID: mdl-33256081
ABSTRACT
High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible, pressure exerts local effects on regions or domains of a protein containing internal voids, contrary to heat or chemical denaturant that destabilize protein structures uniformly. When combined with NMR spectroscopy, high pressure (HP) allows one to monitor at a residue-level resolution the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. The use of HP-NMR has long been hampered by technical difficulties. Owing to the recent development of commercially available high-pressure sample cells, HP-NMR experiments can now be routinely performed. This review summarizes recent advances of HP-NMR techniques for the characterization at a quasi-atomic resolution of the protein folding energy landscape.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Pressure
/
Protein Conformation
/
Magnetic Resonance Spectroscopy
/
Proteins
/
Models, Molecular
/
Protein Folding
Language:
En
Journal:
Molecules
Journal subject:
BIOLOGIA
Year:
2020
Document type:
Article
Affiliation country: