Article
Influence of proline on the thermostability of the active site and membrane arrangement of transmembrane proteins.
Biophysical journal - 1 Nov 2008
Perálvarez-Marín Alex, Lórenz-Fonfría Victor A, Simón-Vázquez Rosana, Gomariz Maria, Meseguer Inmaculada, Querol Enric, Padrós Esteve
Abstract excerpt
Proline residues play a fundamental and subtle role in the dynamics, structure, and function in many membrane proteins. Temperature derivative spectroscopy and differential scanning calorimetry have been used to determine the effect of proline substitution in the structural stability of the active site and transmembrane arrangement of bacteriorhodopsin. We have analyzed the Pro-to-Ala mutation for the...
Topics
- Absorptiometry, Photon
- Archaeal Proteins
- Calorimetry, Differential Scanning
- Catalytic Domain
- Cell Membrane
- Computational Biology
- Halobacterium salinarum
- Membrane Proteins
- Mutant Proteins
- Mutation
- Proline
- Protein Denaturation
- Protein Folding