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- W1536836616 endingPage "240" @default.
- W1536836616 startingPage "163" @default.
- W1536836616 abstract "Protein folding is a process by which a polypeptide chain acquires its native structure from an unfolded state through a transition state. Recent studies of the unfolded states of proteins are based on a modification of the random coil model, recognizing that in many cases some residual native or non-native structure persists.. Combined evidence from the theoretical study of a blocked alanine peptide in aqueous solution and a variety of spectroscopic studies, including ultraviolet circular dichroism (CD), nuclear magnetic resonance (NMR), two-dimensional vibrational spectroscopy, vibrational circular dichroism (VCD), and vibrational Raman optical activity (VROA) reveal that the polyproline II (PII) conformation is the dominant conformation in a variety of short model peptides. This chapter discusses the evidence from short peptides. It reviews the circular dichroism of unfolded proteins and addresses the role of PII in unfolded proteins." @default.
- W1536836616 created "2016-06-24" @default.
- W1536836616 creator A5003547895 @default.
- W1536836616 creator A5010672946 @default.
- W1536836616 creator A5039915636 @default.
- W1536836616 date "2002-01-01" @default.
- W1536836616 modified "2023-10-16" @default.
- W1536836616 title "Is polyproline II a major backbone conformation in unfolded proteins?" @default.
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