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- W2136148049 endingPage "90" @default.
- W2136148049 startingPage "51" @default.
- W2136148049 abstract "Publisher Summary To understand the behavior of unfolded proteins it is necessary to employ experimental techniques able to discriminate between the dynamic true random coil state and more static types of disorder, including situations in which some ordered secondary structure might be present. One such technique is a novel chiroptical spectroscopy called Raman optical activity (ROA). This chapter reviews the application of ROA to studies of unfolded proteins. Because many discrete structure-sensitive bands are present in protein ROA spectra, the technique provides a fresh perspective on the structure and behavior of unfolded proteins and of unfolded sequences in proteins such as A-gliadin and prions that contain distinct structured and unstructured domains. It also provides new insight into the complexity of order in molten globule and reduced protein states and of the more mobile sequences in fully folded proteins such as β-lactoglobulin. The power of ROA in this area derives from the fact that, like the complementary technique of vibrational circular dichroism (VCD), it is a form of vibrational optical activity and so is sensitive to chirality associated with all the 3N−6 fundamental molecular vibrational transitions, where N is the number of atoms." @default.
- W2136148049 created "2016-06-24" @default.
- W2136148049 creator A5066675526 @default.
- W2136148049 creator A5075072917 @default.
- W2136148049 creator A5090469996 @default.
- W2136148049 date "2002-01-01" @default.
- W2136148049 modified "2023-10-16" @default.
- W2136148049 title "Unfolded proteins studied by raman optical activity" @default.
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