Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains

Daidone I, Neuweiler H, Doose S, Sauer M, Smith JC (2010)
PLOS COMPUTATIONAL BIOLOGY 6(1): e1000645.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Characterization of the length dependence of end-to-end loop-closure kinetics in unfolded polypeptide chains provides an understanding of early steps in protein folding. Here, loop-closure in poly-glycine-serine peptides is investigated by combining single-molecule fluorescence spectroscopy with molecular dynamics simulation. For chains containing more than 10 peptide bonds loop-closing rate constants on the 20-100 nanosecond time range exhibit a power-law length dependence. However, this scaling breaks down for shorter peptides, which exhibit slower kinetics arising from a perturbation induced by the dye reporter system used in the experimental setup. The loop-closure kinetics in the longer peptides is found to be determined by the formation of intra-peptide hydrogen bonds and transient beta-sheet structure, that accelerate the search for contacts among residues distant in sequence relative to the case of a polypeptide chain in which hydrogen bonds cannot form. Hydrogen-bond-driven polypeptide-chain collapse in unfolded peptides under physiological conditions found here is not only consistent with hierarchical models of protein folding, that highlights the importance of secondary structure formation early in the folding process, but is also shown to speed up the search for productive folding events.
Erscheinungsjahr
2010
Zeitschriftentitel
PLOS COMPUTATIONAL BIOLOGY
Band
6
Ausgabe
1
Art.-Nr.
e1000645
ISSN
1553-7358
eISSN
1553-7358
Page URI
https://pub.uni-bielefeld.de/record/1588590

Zitieren

Daidone I, Neuweiler H, Doose S, Sauer M, Smith JC. Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains. PLOS COMPUTATIONAL BIOLOGY. 2010;6(1): e1000645.
Daidone, I., Neuweiler, H., Doose, S., Sauer, M., & Smith, J. C. (2010). Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains. PLOS COMPUTATIONAL BIOLOGY, 6(1), e1000645. doi:10.1371/journal.pcbi.1000645
Daidone, I., Neuweiler, H., Doose, S., Sauer, M., and Smith, J. C. (2010). Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains. PLOS COMPUTATIONAL BIOLOGY 6:e1000645.
Daidone, I., et al., 2010. Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains. PLOS COMPUTATIONAL BIOLOGY, 6(1): e1000645.
I. Daidone, et al., “Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains”, PLOS COMPUTATIONAL BIOLOGY, vol. 6, 2010, : e1000645.
Daidone, I., Neuweiler, H., Doose, S., Sauer, M., Smith, J.C.: Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains. PLOS COMPUTATIONAL BIOLOGY. 6, : e1000645 (2010).
Daidone, Isabella, Neuweiler, Hannes, Doose, Soeren, Sauer, Markus, and Smith, Jeremy C. “Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains”. PLOS COMPUTATIONAL BIOLOGY 6.1 (2010): e1000645.

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