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Comment
. 2009 Feb 3;106(5):1299-300.
doi: 10.1073/pnas.0812577106. Epub 2009 Jan 27.

Waltzing alpha-helices

Affiliations
Comment

Waltzing alpha-helices

Victor Muñoz et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Stochastic kinetic simulations of α-helix formation in a 20-residue peptide according to nucleation–elongation theory. The rectangles show 50-ns segments showcasing the 3 basic helix motions: green, stretching-shrinking; blue, sliding; red, splitting-merging. The white vertical frame represents a 5-residue observation window in the Fierz et al. experiment. In principle, the experiment monitors the average time the 5 residues stay in helical conformation (green, blue, or red), or in the coil conformation that allows contact between the 2 probes (uncolored). The simulations, which are performed with single residue rotation rates estimated from T-jump experiments, are nicely consistent with the Fierz et al. results (6). These simulations also highlight that fully exploiting this exciting technique will likely require precisely determining the probe-to-probe contact probability of the rather common conformations with helix and coil residues within the observation window (e.g., the 330- to 345-ns segment in the green simulation).

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References

    1. Bierzynski A, Kim PS, Baldwin RL. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc Natl Acad Sci USA. 1982;79:2470–2474. - PMC - PubMed
    1. Muñoz V, Serrano L. Helix design, prediction and stability. Curr Opin Biotech. 1995;6:383–386. - PubMed
    1. Chakrabartty A, Baldwin RL. Stability of alpha-helices. Adv Protein Chem. 1995;46:141–176. - PubMed
    1. Eaton WA, et al. Fast kinetics and mechanisms in protein folding. Annu Rev Biophys Biomol Struct. 2000;29:327–359. - PMC - PubMed
    1. Huang CY, Getahun Z, Wang T, DeGrado WF, Gai F. Time-resolved infrared study of the helix-coil transition using C-13-labeled helical peptides. J Am Chem Soc. 2001;123:12111–12112. - PubMed

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