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Proceedings Paper

Structure and dynamics of chain-folding initiation sites in ribonuclease A
Author(s): Harold A. Scheraga; J. M. Beals; D. R. Buckler; Elisha Haas; S. Krausz
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Paper 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.

Paper Details

Date Published: 1 April 1992
PDF: 4 pages
Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); doi: 10.1117/12.58263
Show Author Affiliations
Harold A. Scheraga, Cornell Univ. (United States)
J. M. Beals, Cornell Univ. (United States)
D. R. Buckler, Cornell Univ. (United States)
Elisha Haas, Bar-Ilan Univ. (Israel)
S. Krausz, Bar-Ilan Univ. (Israel)


Published in SPIE Proceedings Vol. 1640:
Time-Resolved Laser Spectroscopy in Biochemistry III
Joseph R. Lakowicz, Editor(s)

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