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

L. Pollack, M. W. Tate, A. C. Finnefrock, C. Kalidas, S. Trotter, N. C. Darnton, L. Lurio, R. H. Austin, C. A. Batt, S. M. Gruner, and S. G. J. Mochrie
Phys. Rev. Lett. 86, 4962 – Published 21 May 2001
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Abstract

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.

  • Received 10 September 2000

DOI:https://doi.org/10.1103/PhysRevLett.86.4962

©2001 American Physical Society

Authors & Affiliations

L. Pollack1,*, M. W. Tate1, A. C. Finnefrock1, C. Kalidas2, S. Trotter2, N. C. Darnton3, L. Lurio4, R. H. Austin3, C. A. Batt2, S. M. Gruner1, and S. G. J. Mochrie4

  • 1Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, New York 14853
  • 2Nanobiotechnology Center, Cornell University, Ithaca, New York 14853
  • 3Department of Physics, Princeton University, Princeton, New Jersey 08544
  • 4Department of Physics, MIT, Cambridge, Massachusetts 02139

  • *Permanent address: School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853.

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Vol. 86, Iss. 21 — 21 May 2001

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