Premium
Global Replacement of Tryptophan with Aminotryptophans Generates Non‐Invasive Protein‐Based Optical pH Sensors
Author(s) -
Budisa Nediljko,
Rubini Marina,
Bae Jae H.,
Weyher Elisabeth,
Wenger Waltraud,
Golbik Ralph,
Huber Robert,
Moroder Luis
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20021104)41:21<4066::aid-anie4066>3.0.co;2-6
Subject(s) - tryptophan , chemistry , biophysics , nanotechnology , biochemistry , computer science , materials science , amino acid , biology
Functional protein design : Replacement of the tryptophan indole moiety in proteins with aminoindoles converts pH‐insensitive into pH‐sensitive fluorescent proteins (see picture). Such global substitution of residues in target proteins by noncanonical amino acids with defined spectral properties offers a unique approach for the design of protein‐based molecular sensors.