What is the role of non-native intermediates of beta-lactoglobulin in protein folding?
The mechanism of alpha-->beta transition in folding of beta-lactoglobulin is discussed based on free energy landscape analysis of a long lattice model. It is found that helical propensity of beta-lactoglobulin is driven by conformational entropy and is intrinsically coded in its native structure. We propose a view on a role of folding intermediate, which is "on-pathway" but rich in non-native structures. The present results suggest that the native structure topology plays an important role in alpha-->beta transition.
Chikenji
G
G
Department of Physics, Graduate School of Science, Osaka University, Toyonaka 560-0043, Japan. chikenji@acty.phys.sci.osakau.ac.jp
Kikuchi
M
M
D003198:Computer Simulation; D004735:Energy Transfer; D007782:Lactoglobulins / Q000737:chemistry*; D008958:Models, Molecular; D009010:Monte Carlo Method; D017510:Protein Folding; D017433:Protein Structure, Secondary
D007782:Lactoglobulins