THE PHOTOPHYSICAL PROBE, 7‐AZATRYPTOPHAN, IN SYNTHETIC PEPTIDES

K. L. Rich; M. Négrerie; J. Li; S. Elliott; R. W. Thornburg; J. W. Petrich

doi:10.1111/j.1751-1097.1993.tb04898.x

THE PHOTOPHYSICAL PROBE, 7‐AZATRYPTOPHAN, IN SYNTHETIC PEPTIDES

K. L. Rich
, M. Négrerie
, J. Li
, S. Elliott
, R. W. Thornburg
, J. W. Petrich

Research output: Contribution to journal › Article › peer-review

Abstract

7‐Azatryptophan is proposed as an alternative to tryptophan as a photophysical probe in the study of protein structure and dynamics. Not only are the spectral characteristics of 7‐azatryptophan easily distinguishable from those of tryptophan, but this nonnatural amino acid is shown to be amenablc to incorporation into peptides. We present the first synthesis and purification of a synthetic peptide containing 7‐azatryptophan, NAc‐Pro‐7‐azatryptophan‐Asn‐NH₂, which is shown to be a competitive inhibitor of α‐chymotrysin.

Original language	English
Pages (from-to)	28-30
Number of pages	3
Journal	Photochemistry and Photobiology
Volume	58
Issue number	1
DOIs	https://doi.org/10.1111/j.1751-1097.1993.tb04898.x
Publication status	Published - 1 Jan 1993
Externally published	Yes

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title = "THE PHOTOPHYSICAL PROBE, 7‐AZATRYPTOPHAN, IN SYNTHETIC PEPTIDES",

abstract = "7‐Azatryptophan is proposed as an alternative to tryptophan as a photophysical probe in the study of protein structure and dynamics. Not only are the spectral characteristics of 7‐azatryptophan easily distinguishable from those of tryptophan, but this nonnatural amino acid is shown to be amenablc to incorporation into peptides. We present the first synthesis and purification of a synthetic peptide containing 7‐azatryptophan, NAc‐Pro‐7‐azatryptophan‐Asn‐NH2, which is shown to be a competitive inhibitor of α‐chymotrysin.",

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doi = "10.1111/j.1751-1097.1993.tb04898.x",

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AU - Rich, K. L.

AU - Négrerie, M.

AU - Li, J.

AU - Elliott, S.

AU - Thornburg, R. W.

AU - Petrich, J. W.

PY - 1993/1/1

Y1 - 1993/1/1

N2 - 7‐Azatryptophan is proposed as an alternative to tryptophan as a photophysical probe in the study of protein structure and dynamics. Not only are the spectral characteristics of 7‐azatryptophan easily distinguishable from those of tryptophan, but this nonnatural amino acid is shown to be amenablc to incorporation into peptides. We present the first synthesis and purification of a synthetic peptide containing 7‐azatryptophan, NAc‐Pro‐7‐azatryptophan‐Asn‐NH2, which is shown to be a competitive inhibitor of α‐chymotrysin.

AB - 7‐Azatryptophan is proposed as an alternative to tryptophan as a photophysical probe in the study of protein structure and dynamics. Not only are the spectral characteristics of 7‐azatryptophan easily distinguishable from those of tryptophan, but this nonnatural amino acid is shown to be amenablc to incorporation into peptides. We present the first synthesis and purification of a synthetic peptide containing 7‐azatryptophan, NAc‐Pro‐7‐azatryptophan‐Asn‐NH2, which is shown to be a competitive inhibitor of α‐chymotrysin.

U2 - 10.1111/j.1751-1097.1993.tb04898.x

DO - 10.1111/j.1751-1097.1993.tb04898.x

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SP - 28

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JO - Photochemistry and Photobiology

JF - Photochemistry and Photobiology

IS - 1

ER -

THE PHOTOPHYSICAL PROBE, 7‐AZATRYPTOPHAN, IN SYNTHETIC PEPTIDES

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