Origins of barriers and barrierless folding in BBL.
In contrast to classical chemical phenomenology, theory suggests that proteins may undergo downhill folding without an activation barrier under certain thermodynamic conditions. Recently, the BBL protein was proposed to fold by such a downhill scenario, but discrepancies between experimental results found in different groups argue against this. After briefly reviewing the major experimental studies of the BBL folding mechanism, we show that simulations of both coarse-grained and atomistic models can reconcile the seemingly conflicting observations.
Cho
Samuel S
SS
Center for Theoretical Biological Physics and Departments of Chemistry and Biochemistry and Physics, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Weinkam
Patrick
P
Wolynes
Peter G
PG
D000217:Acyltransferases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001671:Biochemistry / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008962:Models, Theoretical; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics
D000217:Acyltransferases; C021515:dihydrolipoamide succinyltransferase