Protein folding intermediates

Ducin Y and P A Kollrtran 1998. Pathways to a Protein Folding Intermediate Observed in Microsecond Simulation in Aqueous Solution. Science 282 740-744. 

Y Duan, PA Kollman. Pathways to a protein folding intermediate observed in a 1-microsecond simulation m aqueous solution. Science 282 740-744, 1998. 

Initial protein folding intermediates formed as a consequence of nonlocal interactions on the reaction path from unfolded to partially folded states. These loops are likely to determine the trajectory of later folding steps. The character of nonlocal interactions is likely to be much different than structures inferred from the results... 

Bai, Y., T.R. Sosnick, L. Mayne, and S.W. Englander (1996). Protein-folding intermediates Native-state hydrogen-exchange. Science 269 192-197. 

Roder, H. (1989). Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. In Methods in Enzymology (N. J. Oppen-heimer and T. L. James, eds.), Vol. 176, pp. 446-473. Academic Press, Orlando, FL. 

Bai, Y., Sosnick, T. R., Mayne, L. Englander, S. W. (1995). Protein Folding Intermediates Native-State Hydrogen Exchange. Science 269, 192-197. 

Gorovits, B., and Horovits, P. M. (2002) High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure. Biochemistry 37, 6132... 

Englander, S. W. 2000. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 29, 213—238. 

The first millisecond protein HX measurements were made by automated quench-flow pulse labeling and were aimed at characterizing early protein-folding intermediates [15, 16]. In these experiments, unlabeled protein was mixed with D O and incubated for a short period (ms), followed by a rapid pH drop and flash freeze to quench the reaction. Labeled samples were then analyzed by NMR (this was 1988, the same year that John Fenn showed the first electrospray protein mass spectra at the American Society for Mass Spectrometry meeting). Quench-flow HX for protein folding was translated to MS a few years later by Miranker and coworkers [17]. 

Pan, J.X., Han, J., Borchers, C.H., Konermann, L. (2010) Characterizing short-lived protein folding intermediates by top-down hydrogen exchange mass spectrometry. Analytical Chemistry, 82 (20), 8591-8597. 

D. A. Simmons and L. Konermann, Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-hne isotope-pulse labeling. Biochemistry 42, 1906-1914 (2002). 

Simmons, D.A., Konermann, L. (2002) Characterization of Transient Protein Folding Intermediates during Myoglobin Reconstitution by Time-resolved Electrospray Mass Spectrometry with On-hne Isotopic Pulse Labeling. Biochemistry 41 1906-1914. 

R. W. Woody, Circular Dichroism of Protein-Folding Intermediates , in Methods in Enzymology, eds. J. Holt, M. Johnson and G. Ackers, Elsevier, 2004, vol. 380, Energetics of Biological Macromolecules, Part E, p. 242. 

Englander S W, Protein folding intermediates and pathways studied by hydrogen... 

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