Picosecond fluorescence studies of polypeptide dynamics: fluorescence anisotropies and lifetimes

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

doi:10.1016/0009-2614(87)80150-1

Picosecond fluorescence studies of polypeptide dynamics: fluorescence anisotropies and lifetimes

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

^*Corresponding author for this work

Chemistry

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42 Scopus citations

Abstract

Fluorescence lifetimes and anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are reported. The anisotropy data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84 (1986) 510). A persistence length of about 7 to 10 residues is obtained for the mobilities in the two hormones. The theory is able to account for chain length and probe location effects, but the calculated time dependence of the anisotropy does not fit the experimental curve well at short times.

Original language	English (US)
Pages (from-to)	55-61
Number of pages	7
Journal	Chemical Physics Letters
Volume	139
Issue number	1
DOIs	https://doi.org/10.1016/0009-2614(87)80150-1
State	Published - Aug 14 1987

ASJC Scopus subject areas

Physics and Astronomy(all)
Physical and Theoretical Chemistry

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title = "Picosecond fluorescence studies of polypeptide dynamics: fluorescence anisotropies and lifetimes",

abstract = "Fluorescence lifetimes and anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are reported. The anisotropy data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84 (1986) 510). A persistence length of about 7 to 10 residues is obtained for the mobilities in the two hormones. The theory is able to account for chain length and probe location effects, but the calculated time dependence of the anisotropy does not fit the experimental curve well at short times.",

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

note = "Funding Information: This work was supportedb y a grant from the National ScienceF oundation.W e thank Professor Karl Freed for muchh elpfula dvice.J WP was sup-portedb y an NSF IndustrializedC ountriesp ostdoc-toral fellowship,a n INSERM pasteo range,a nd a fellowshipf rom La Fondation pour la Recherche Mtdicale.",

year = "1987",

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doi = "10.1016/0009-2614(87)80150-1",

language = "English (US)",

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T1 - Picosecond fluorescence studies of polypeptide dynamics

T2 - fluorescence anisotropies and lifetimes

AU - Chen, Lin X Q

AU - Petrich, Jacob W.

AU - Fleming, Graham R.

AU - Perico, Angelo

N1 - Funding Information: This work was supportedb y a grant from the National ScienceF oundation.W e thank Professor Karl Freed for muchh elpfula dvice.J WP was sup-portedb y an NSF IndustrializedC ountriesp ostdoc-toral fellowship,a n INSERM pasteo range,a nd a fellowshipf rom La Fondation pour la Recherche Mtdicale.

PY - 1987/8/14

Y1 - 1987/8/14

N2 - Fluorescence lifetimes and anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are reported. The anisotropy data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84 (1986) 510). A persistence length of about 7 to 10 residues is obtained for the mobilities in the two hormones. The theory is able to account for chain length and probe location effects, but the calculated time dependence of the anisotropy does not fit the experimental curve well at short times.

AB - Fluorescence lifetimes and anisotropies for single tryptophan-containing polypeptide hormones ACTH and glucagon, and a series of their fragments are reported. The anisotropy data are discussed in the context of the theory of Perico and Guenza (J. Chem. Phys. 84 (1986) 510). A persistence length of about 7 to 10 residues is obtained for the mobilities in the two hormones. The theory is able to account for chain length and probe location effects, but the calculated time dependence of the anisotropy does not fit the experimental curve well at short times.

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Picosecond fluorescence studies of polypeptide dynamics: fluorescence anisotropies and lifetimes

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