Hole burning Stark-effect studies on aromatic aminoacids: Part II. A comparative investigation of tyrosine and the BPTI-protein

Markus Stübner; Christoph Hecht; Ellen Schneider; Josef Friedrich

doi:10.1039/b208926b

Hole burning Stark-effect studies on aromatic aminoacids: Part II. A comparative investigation of tyrosine and the BPTI-protein

Markus Stübner, Christoph Hecht, Ellen Schneider, Josef Friedrich

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Technical University of Munich

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3 Scopus citations

Abstract

We present hole burning Stark-effect experiments on the aromatic aminoacid tyrosine in a glycerol/water glass. In addition we demonstrate, for the first time, that it is possible to exploit aromatic aminoacids as Stark-labels in proteins. As an example we present experiments with bovine pancreatic trypsin inhibitor (BPTI). We discuss our results in light of recent model calculations on phenol/water complexes.

Original language	English
Pages (from-to)	6080-6085
Number of pages	6
Journal	Physical Chemistry Chemical Physics
Volume	4
Issue number	24
DOIs	https://doi.org/10.1039/b208926b
State	Published - 2002

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title = "Hole burning Stark-effect studies on aromatic aminoacids: Part II. A comparative investigation of tyrosine and the BPTI-protein",

abstract = "We present hole burning Stark-effect experiments on the aromatic aminoacid tyrosine in a glycerol/water glass. In addition we demonstrate, for the first time, that it is possible to exploit aromatic aminoacids as Stark-labels in proteins. As an example we present experiments with bovine pancreatic trypsin inhibitor (BPTI). We discuss our results in light of recent model calculations on phenol/water complexes.",

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AU - Stübner, Markus

AU - Hecht, Christoph

AU - Schneider, Ellen

AU - Friedrich, Josef

PY - 2002

Y1 - 2002

N2 - We present hole burning Stark-effect experiments on the aromatic aminoacid tyrosine in a glycerol/water glass. In addition we demonstrate, for the first time, that it is possible to exploit aromatic aminoacids as Stark-labels in proteins. As an example we present experiments with bovine pancreatic trypsin inhibitor (BPTI). We discuss our results in light of recent model calculations on phenol/water complexes.

AB - We present hole burning Stark-effect experiments on the aromatic aminoacid tyrosine in a glycerol/water glass. In addition we demonstrate, for the first time, that it is possible to exploit aromatic aminoacids as Stark-labels in proteins. As an example we present experiments with bovine pancreatic trypsin inhibitor (BPTI). We discuss our results in light of recent model calculations on phenol/water complexes.

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U2 - 10.1039/b208926b

DO - 10.1039/b208926b

M3 - Article

AN - SCOPUS:2642537410

SN - 1463-9076

VL - 4

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JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

IS - 24

ER -

Hole burning Stark-effect studies on aromatic aminoacids: Part II. A comparative investigation of tyrosine and the BPTI-protein

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