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

H. A. Scheraga; J. M. Beals; D. R. Buckler; E. Haas; S. Krausz

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

H. A. Scheraga, J. M. Beals, D. R. Buckler, E. Haas, S. Krausz

Cornell University

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

1 Scopus citations

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.

Original language	English
Title of host publication	Proceedings of SPIE - The International Society for Optical Engineering
Publisher	Publ by Int Soc for Optical Engineering
Pages	672-675
Number of pages	4
ISBN (Print)	0819407860
State	Published - 1992
Externally published	Yes
Event	Time-Resolved Laser Spectroscopy in Biochemistry III - Los Angeles, CA, USA Duration: 20 Jan 1992 → 22 Jan 1992

Publication series

Name	Proceedings of SPIE - The International Society for Optical Engineering
Volume	1640
ISSN (Print)	0277-786X

Conference

Conference	Time-Resolved Laser Spectroscopy in Biochemistry III
City	Los Angeles, CA, USA
Period	20/01/92 → 22/01/92

Cite this

Scheraga, H. A., Beals, J. M., Buckler, D. R., Haas, E., & Krausz, S. (1992). Structure and dynamics of chain-folding initiation sites in ribonuclease A. In Proceedings of SPIE - The International Society for Optical Engineering (pp. 672-675). (Proceedings of SPIE - The International Society for Optical Engineering; Vol. 1640). Publ by Int Soc for Optical Engineering.

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title = "Structure and dynamics of chain-folding initiation sites in ribonuclease A",

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.",

author = "Scheraga, {H. A.} and Beals, {J. M.} and Buckler, {D. R.} and E. Haas and S. Krausz",

year = "1992",

language = "אנגלית",

isbn = "0819407860",

series = "Proceedings of SPIE - The International Society for Optical Engineering",

publisher = "Publ by Int Soc for Optical Engineering",

pages = "672--675",

booktitle = "Proceedings of SPIE - The International Society for Optical Engineering",

note = "Time-Resolved Laser Spectroscopy in Biochemistry III ; Conference date: 20-01-1992 Through 22-01-1992",

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Scheraga, HA, Beals, JM, Buckler, DR, Haas, E & Krausz, S 1992, Structure and dynamics of chain-folding initiation sites in ribonuclease A. in Proceedings of SPIE - The International Society for Optical Engineering. Proceedings of SPIE - The International Society for Optical Engineering, vol. 1640, Publ by Int Soc for Optical Engineering, pp. 672-675, Time-Resolved Laser Spectroscopy in Biochemistry III, Los Angeles, CA, USA, 20/01/92.

Structure and dynamics of chain-folding initiation sites in ribonuclease A. / Scheraga, H. A.; Beals, J. M.; Buckler, D. R. et al.
Proceedings of SPIE - The International Society for Optical Engineering. Publ by Int Soc for Optical Engineering, 1992. p. 672-675 (Proceedings of SPIE - The International Society for Optical Engineering; Vol. 1640).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

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T1 - Structure and dynamics of chain-folding initiation sites in ribonuclease A

AU - Scheraga, H. A.

AU - Beals, J. M.

AU - Buckler, D. R.

AU - Haas, E.

AU - Krausz, S.

PY - 1992

Y1 - 1992

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AB - 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.

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T3 - Proceedings of SPIE - The International Society for Optical Engineering

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BT - Proceedings of SPIE - The International Society for Optical Engineering

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T2 - Time-Resolved Laser Spectroscopy in Biochemistry III

Y2 - 20 January 1992 through 22 January 1992

ER -

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

Abstract

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Conference

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