Phys. Rev. Lett. 86, 4962–4965 (2001)Time Resolved Collapse of a Folding Protein Observed with Small Angle X-Ray ScatteringReceived 10 September 2000; published in the issue dated 21 May 2001 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 β-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. © 2001 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.86.4962
DOI:
10.1103/PhysRevLett.86.4962
PACS:
87.14.Ee, 87.15.He
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