An alpha-helical burst in the src SH3 folding pathway.
Src SH3 is a small all-beta-sheet protein composed of a single domain. We studied the folding behavior of src SH3 at various conditions by circular dichroism (CD), fluorescence, and X-ray solution scattering methods. On the src SH3 folding pathway, an alpha-helix-rich intermediate appeared not only at subzero temperatures but also above 0 degrees C. The fraction of alpha-helix in the kinetically observed intermediate is ca. 26% based on the kinetic CD experiment. X-ray solution scattering revealed that the intermediate was compact but not fully packed. The analysis of CD implies that the amplitude of the burst phase is proportional to the helical fraction calculated according to the helix-coil transition theory. This strongly suggests that the initial folding core is formed by the collapse of much less stably existing alpha-helices.
Li
Jinsong
J
Departments of Physics, Kansai Medical University, 18-89 Uyama-Higashi, Hirakata 573-1136, Japan.
Shinjo
Masaji
M
Matsumura
Yoshitaka
Y
Morita
Masayuki
M
Baker
David
D
Ikeguchi
Masamichi
M
Kihara
Hiroshi
H
D002942:Circular Dichroism; D004926:Escherichia coli / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D018909:src Homology Domains
D011994:Recombinant Proteins