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- W1970202379 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.
- W1970202379 created "2016-06-24" @default.
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- W1970202379 date "1968-11-01" @default.
- W1970202379 modified "2023-10-11" @default.
- W1970202379 title "Similarity in backbone conformation of egg white lysozyme and bovine α lactalbumin" @default.
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- W1970202379 doi "https://doi.org/10.1016/0006-291x(68)90327-6" @default.
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