Time resolved collapse of a folding protein observed with small angle x-ray scattering.
High-intensity, "pink" beam from an undulator was used in conjunction with microfabricated rapid-fluid mixing devices to monitor the early events in protein folding with time resolved small angle x-ray scattering. This Letter describes recent work on the protein bovine beta-lactoglobulin where collapse from an expanded to a compact set of states was directly observed on the millisecond time scale. The role of chain collapse, one of the initial stages of protein folding, is not currently understood. The characterization of transient, compact states is vital in assessing the validity of theories and models of the folding process.
Pollack
L
L
Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, New York 14853, USA.
Tate
M W
MW
Finnefrock
A C
AC
Kalidas
C
C
Trotter
S
S
Darnton
N C
NC
Lurio
L
L
Austin
R H
RH
Batt
C A
CA
Gruner
S M
SM
Mochrie
S G
SG
D000818:Animals; D002417:Cattle; D007782:Lactoglobulins / Q000737:chemistry*; D017510:Protein Folding; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D014965:X-Rays
D007782:Lactoglobulins