Time resolved collapse of a folding protein observed with small angle x-ray scattering

被引:145
作者
Pollack, L [1 ]
Tate, MW
Finnefrock, AC
Kalidas, C
Trotter, S
Darnton, NC
Lurio, L
Austin, RH
Batt, CA
Gruner, SM
Mochrie, SGJ
机构
[1] Cornell Univ, Atom & Solid State Phys Lab, Ithaca, NY 14853 USA
[2] Cornell Univ, Nanobiotechnol Ctr, Ithaca, NY 14853 USA
[3] Princeton Univ, Dept Phys, Princeton, NJ 08544 USA
[4] MIT, Dept Phys, Cambridge, MA 02139 USA
关键词
D O I
10.1103/PhysRevLett.86.4962
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
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 P-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.
引用
收藏
页码:4962 / 4965
页数:4
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