Picosecond Fluorescence Studies of Polypeptide Dynamics

Lin X.Q. Chen; Jacob W. Petrich; Angelo Perico; Graham R. Fleming

doi:10.1117/12.945391

Picosecond Fluorescence Studies of Polypeptide Dynamics

Lin X.Q. Chen^*, Jacob W. Petrich, Angelo Perico, Graham R. Fleming

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Conference article › peer-review

Abstract

Fluorescence anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are studied. The data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84, 510 (1986)) and a persistence length of about 7 to 10 residues obtained for the mobilities in the two hormones. Theory is able to account for chain length and probe location effects very well. The observed discrepencies between calculated and measured anisotropy decays very likely arise from approximations made in the calculation and from the limited time resolution of the experiments.

Original language	English (US)
Pages (from-to)	216-222
Number of pages	7
Journal	Proceedings of SPIE - The International Society for Optical Engineering
Volume	909
DOIs	https://doi.org/10.1117/12.945391
State	Published - Jun 24 1988
Event	Time-Resolved Laser Spectroscopy in Biochemistry 1988 - Los Angeles, United States Duration: Jan 11 1988 → Jan 17 1988

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Condensed Matter Physics
Computer Science Applications
Applied Mathematics
Electrical and Electronic Engineering

Access to Document

10.1117/12.945391

Cite this

@article{418565523bd94959979433cc64ce999f,

title = "Picosecond Fluorescence Studies of Polypeptide Dynamics",

abstract = "Fluorescence anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are studied. The data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84, 510 (1986)) and a persistence length of about 7 to 10 residues obtained for the mobilities in the two hormones. Theory is able to account for chain length and probe location effects very well. The observed discrepencies between calculated and measured anisotropy decays very likely arise from approximations made in the calculation and from the limited time resolution of the experiments.",

author = "Chen, {Lin X.Q.} and Petrich, {Jacob W.} and Angelo Perico and Fleming, {Graham R.}",

year = "1988",

month = jun,

day = "24",

doi = "10.1117/12.945391",

language = "English (US)",

volume = "909",

pages = "216--222",

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

issn = "0277-786X",

publisher = "SPIE",

}

TY - JOUR

T1 - Picosecond Fluorescence Studies of Polypeptide Dynamics

AU - Chen, Lin X.Q.

AU - Petrich, Jacob W.

AU - Perico, Angelo

AU - Fleming, Graham R.

PY - 1988/6/24

Y1 - 1988/6/24

N2 - Fluorescence anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are studied. The data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84, 510 (1986)) and a persistence length of about 7 to 10 residues obtained for the mobilities in the two hormones. Theory is able to account for chain length and probe location effects very well. The observed discrepencies between calculated and measured anisotropy decays very likely arise from approximations made in the calculation and from the limited time resolution of the experiments.

AB - Fluorescence anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are studied. The data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84, 510 (1986)) and a persistence length of about 7 to 10 residues obtained for the mobilities in the two hormones. Theory is able to account for chain length and probe location effects very well. The observed discrepencies between calculated and measured anisotropy decays very likely arise from approximations made in the calculation and from the limited time resolution of the experiments.

UR - http://www.scopus.com/inward/record.url?scp=85075140011&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85075140011&partnerID=8YFLogxK

U2 - 10.1117/12.945391

DO - 10.1117/12.945391

M3 - Conference article

AN - SCOPUS:85075140011

SN - 0277-786X

VL - 909

SP - 216

EP - 222

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

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

T2 - Time-Resolved Laser Spectroscopy in Biochemistry 1988

Y2 - 11 January 1988 through 17 January 1988

ER -

Picosecond Fluorescence Studies of Polypeptide Dynamics

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this