Induction of helical conformation in all beta-sheet proteins by trifluoroethanol.
The effect of 2,2,2-Trifluoroethanol (TFE) on the structure of five all beta-sheet proteins, isolated from the venom of the Taiwan cobra (Naja naja atra), is studied. In all the toxins used, it is observed that significant amount of alpha-helix is induced at higher concentrations of TFE. In all these proteins, the induction of helical conformation and disruption of the tertiary structure seem to occur simultaneously. The structural transitions induced by TFE in reduced and denatured protein appear to be different from those observed in the native protein(s). In our opinion, the findings reported herein could have significant implications on research in the area of protein folding.
Arunkumar
A I
AI
Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.
Kumar
T K
TK
Jayaraman
G
G
Samuel
D
D
Yu
C
C
D002942:Circular Dichroism; D004179:Cobra Cardiotoxin Proteins / Q000737:chemistry* / Q000378:metabolism; D003039:Cobra Neurotoxin Proteins / Q000737:chemistry* / Q000378:metabolism; D004220:Disulfides; D004546:Elapid Venoms / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D014270:Trifluoroethanol / Q000737:chemistry* / Q000378:metabolism; D014466:Ultraviolet Rays
D004179:Cobra Cardiotoxin Proteins; D003039:Cobra Neurotoxin Proteins; D004220:Disulfides; D004546:Elapid Venoms; C082541:cardiotoxin V; D014270:Trifluoroethanol