Folding and stability of globular proteins and implications for function.
The description of protein folding pathways and the principles that govern them has proven to be one of the most difficult problems to be solved in structural biology. But the combination of experiments and simulations has now provided a clearer picture of the chemistry involved. Once folded, however, proteins remain dynamic systems making possible both small-scale and large-scale structural and/or dynamical changes upon binding or releasing of ligands and during catalysis. In this review we focus on recent advances in the field of protein folding and discuss possible links between folding, stability, and binding dynamics.
Travaglini-Allocatelli
Carlo
C
Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza Università di Roma, Piazzale A. Moro 5, 00185 Rome, Italy.
Ivarsson
Ylva
Y
Jemth
Per
P
Gianni
Stefano
S
D000818:Animals; D001665:Binding Sites; D006801:Humans; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D011506:Proteins