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NMR Characterization of a Peptide Model Provides Evidence for Significant Structure in the Unfolded State of the Villin Headpiece Helical Subdomain †

✍ Scribed by Tang, Yuefeng; Goger, Michael J.; Raleigh, Daniel P.

Book ID
126861958
Publisher
American Chemical Society
Year
2006
Tongue
English
Weight
369 KB
Volume
45
Category
Article
ISSN
0006-2960

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Solution structure of a peptide model of
Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of nonnative structure in the denatured state
✍ Stephen J. Demarest; Daniel P. Raleigh 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 373 KB 👁 1 views

Elucidating the properties of the denatured state of proteins under conditions relevant for their folding is a key factor in understanding the folding process. We show that a peptide corresponding to residues 111-120 of human ␣-lactalbumin has a pronounced propensity to adopt nonnative structure in