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Comment
. 1993 Nov 5;262(5135):848-9.
doi: 10.1126/science.8235606.

In pursuit of protein folding

S W Englander  1
Affiliations
Comment

In pursuit of protein folding

S W Englander. Science. .
No abstract available

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Figures

Figure
Figure. Stalking a folding protein
The HX pulse labeling experiment. Folding proceeds from the random coil (left) through intermediate forms (middle) to the native state (right). Pulsed H-D exchange is used to label the protein in a time-resolved and structurally sensitive way while it refolds. Analysis of the refolded native protein by two-dimensional NMR or mass spectrometry (or both) can then provide kinetic and structural information on transient intermediates in the folding process.
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Comment on

References

    1. Miranker A, Robinson CV, Radford SE, Aplin RT, Dobson CM. Science. 1993;262:896. - PubMed
    1. Jennings PA, Wright PE. :892. ibid.
    1. Mayo SL, Baldwin RL. :873. ibid.
    1. Baldwin RL. Curr Opin Struct Biol. 1993;3:84.
    2. Englander SW, Mayne L. Annu Rev Biophys Biomol Struct. 1992;21:243. - PubMed
    3. Elove GA, Roder H. Frontiers in Protein Folding. In: Georgiou G, editor. ACS Symposium Series 470. American Chemical Society; Washington, DC: 1991. pp. 50–63.
    1. Englander SW, Kallenbach NR. Q Rev Biophys. 1984;16:521. - PubMed