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Site-Specific Folding Dynamics of Isotopically Labeled Peptides Studied by Time-Resolved Infrared-Spectroscopy

✍ Scribed by Krejtschi, Carsten; Wu, Ling; Huang, Rong; Hauser, Karin; Keiderling, Timothy A.


Book ID
119204816
Publisher
Biophysical Society
Year
2009
Tongue
English
Weight
39 KB
Volume
96
Category
Article
ISSN
0006-3495

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Time resolved fluorescence was used to study the dynamics on the nanosecond and subnanosecond time scale of the peptide hormone motilin. The peptide is composed of 22 amino acid residues and has one tyrosine residue in position 7, which was used as an intrinsic fluorescence probe. The measurements s