Structure and dynamics of chain-folding initiation sites in ribonuclease A

Harold A. Scheraga; J. M. Beals; D. R. Buckler; Elisha Haas; S. Krausz

doi:10.1117/12.58263

1 April 1992 Structure and dynamics of chain-folding initiation sites in ribonuclease A

Harold A. Scheraga, J. M. Beals, D. R. Buckler, Elisha Haas, S. Krausz

Proceedings Volume 1640, Time-Resolved Laser Spectroscopy in Biochemistry III; (1992) https://doi.org/10.1117/12.58263
Event: OE/LASE '92, 1992, Los Angeles, CA, United States

Abstract

The tryptic peptide OT-16 of oxidized ribonuclease A, which consist of the 20 C-terminal amino acid residues of the protein, is thought to contain a chain-folding-initiation-site at residues 106 - 118. Non-radiative energy transfer has been used to assess the structure and dynamics of this peptide alone, and conjugated to another fragment of the ribonuclease molecule, in solution. Preliminary work has also been carried out on the S-peptide of ribonuclease A.

Citation Download Citation

Harold A. Scheraga, J. M. Beals, D. R. Buckler, Elisha Haas, and S. Krausz "Structure and dynamics of chain-folding initiation sites in ribonuclease A", Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); https://doi.org/10.1117/12.58263

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