Time Resolved Collapse of a Folding Protein Observed with Small Angle X-Ray Scattering

Journal Article · Mon May 21 00:00:00 EDT 2001 · Physical Review Letters

DOI:https://doi.org/10.1103/PhysRevLett.86.4962· OSTI ID:40205853

Pollack, L; Tate, M W; Finnefrock, A C; Kalidas, C; Trotter, S; Darnton, N C; Lurio, L; Austin, R H; Batt, C A; Gruner, S M ^[1]

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1. and others

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.

• Sponsoring Organization: (US)
• OSTI ID: 40205853
• Journal Information: Physical Review Letters, Vol. 86, Issue 21; Other Information: DOI: 10.1103/PhysRevLett.86.4962; Othernumber: PRLTAO000086000021004962000001; 061121PRL; PBD: 21 May 2001; ISSN 0031-9007
• Publisher: The American Physical Society
• Country of Publication: United States
• Language: English

Related Subjects

43 PARTICLE ACCELERATORS
CATTLE
CHAINS
MONITORS
PROTEINS
SCATTERING
WIGGLER MAGNETS