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In 1981, Lubert Stryer (1938–2024) emphasized that protein molecules are not inflexible crystal-like entities, but are characterized by very rapid motions of selected regions, since nanosecond fluorescence polarization analysis revealed that segmental flexibility, where domains can rotate over an appreciable angular range of times of nanoseconds, is a characteristic feature of multidomain proteins, whereas time-resolved fluorescence polarization studies have demonstrated that internal tryptophan residues can be flexible in the subnanosecond time range (Stryer, 1981)
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