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Journal ArticleDOI

Benzophenone photophores in biochemistry

György Dormán, +1 more
- 17 May 1994 - 
- Vol. 33, Iss: 19, pp 5661-5673
TLDR
This Perspectives includes a brief review of BP photochemistry and a selection of specific applications of these photoprobes, which address questions in protein, nucleic acid, and lipid biochemistry.
Abstract
The photoactivatable aryl ketone derivatives have been rediscovered as biochemical probes in the last 5 years. The expanding use of benzophenone (BP) photoprobes can be attributed to three distinct chemical and biochemical advantages. First, BPs are chemically more stable than diazo esters, aryl azides, and diazirines. Second, BPs can be manipulated in ambient light and can be activated at 350-360 nm, avoiding protein-damaging wavelengths. Third, BPs react preferentially with unreactive C-H bonds, even in the presence of solvent water and bulk nucleophiles. These three properties combine to produce highly efficient covalent modifications of macromolecules, frequently with remarkable site specificity. This Perspectives includes a brief review of BP photochemistry and a selection of specific applications of these photoprobes, which address questions in protein, nucleic acid, and lipid biochemistry.

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Citations
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Journal ArticleDOI

Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli

TL;DR: An orthogonal aminoacyl-tRNA synthetase/tRNA pair is evolved that makes possible the in vivo incorporation of p-benzoyl-l-phenylalanine into proteins in Escherichia coli in response to the amber codon, TAG.
Journal ArticleDOI

Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions.

TL;DR: The most popular cross-linking reagents for protein structure analysis are described and an overview of the different available strategies that employ chemical cross- linking and different mass spectrometric techniques are given.
Journal ArticleDOI

Skin-inspired hydrogel-elastomer hybrids with robust interfaces and functional microstructures

TL;DR: Zhao et al. as discussed by the authors proposed a simple yet versatile method to assemble hydrogels and elastomers into hybrids with extremely robust interfaces (interfacial toughness over 1,000 Jm−2) and functional microstructures such as microfluidic channels and electrical circuits.
Journal ArticleDOI

Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light.

TL;DR: The de novo design and development of a type of protein cross-linking reaction that uses a photogenerated oxidant to mediate rapid and efficient cross- linking of associated proteins.
Journal ArticleDOI

Using photolabile ligands in drug discovery and development.

TL;DR: Examples are presented from three fundamentally different approaches: (1) photoaffinity labeling of target macromolecules; (2) photoactivation and release of 'caged ligands'; and (3) photoimmobilization of ligands onto surfaces.
References
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Journal ArticleDOI

Multiplexed biochemical assays with biological chips

TL;DR: High density peptide and oligonucleotide chips are fabricated using semiconductor-based technologies and have a variety of biological applications.
Journal ArticleDOI

New Photolabeling and Crosslinking Methods

TL;DR: The author revealed that photo-activatable Phospholipids as Photo-affinity Probes as well as the properties of Reactive Amino Acid Residues and Photolabeling of Membranes had changed in the last decade.
Journal ArticleDOI

Biomimetic control of chemical selectivity

TL;DR: A number of enzyme mimics have been constructed to imitate an enzymatic mechanism, using the same catalytic groups which the enzyme uses and examining the question of whether a proposed mechanism for the enzyme process is reasonable or duplicable as discussed by the authors.
Book ChapterDOI

Biomimetic control of chemical selectivity

TL;DR: One of the challenges for enzyme mimics is to duplicate not only the mechanism by which the enzyme operates but also the very large rate of the process.
Journal ArticleDOI

p-Benzoyl-L-phenylalanine, a new photoreactive amino acid. Photolabeling of calmodulin with a synthetic calmodulin-binding peptide.

TL;DR: A new photoreactive amino acid analog, p-benzoyl-L-phenylalanine, is described and its utility was illustrated in place of tryptophan in a 17-residue calmodulin-binding peptide.
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