scholarly journals Activity-based ubiquitin-protein probes reveal target protein specificity of deubiquitinating enzymes

2018 ◽  
Vol 9 (40) ◽  
pp. 7859-7865 ◽  
Author(s):  
Ping Gong ◽  
Gregory A. Davidson ◽  
Weijun Gui ◽  
Kun Yang ◽  
William P. Bozza ◽  
...  
Keyword(s):  
Target Protein ◽  
Deubiquitinating Enzymes ◽  
Site Specific ◽  
Protein Specificity

Activity-based Ub-PCNA probes identify deubiquitinating enzymes (DUBs) specific for PCNA and demonstrate site-specific deubiquitination by DUBs.

scholarly journals Flavin-Tag: A Facile Method for Site-Specific Labeling of Proteins with a Flavin Fluorophore

2021 ◽  
Author(s):  
Yapei Tong ◽  
Misun Lee ◽  
Jeroen Drenth ◽  
Marco Fraaije
Keyword(s):  
Target Protein ◽  
Protein Labeling ◽  
Flexible Tool ◽  
Site Specific ◽  
Short Peptide

<p>Flavin-tag: we developed a facile method to label a target protein with a flavin. By using a short peptide (Flavin-tag), recognized by a flavinylating enzyme, FMN can be covalently incorporated. Attachment of the flavin chromo- and fluorophore can be performed <i>in vivo</i> and <i>in vitro</i> rendering the Flavin-tag a flexible tool for protein labeling.</p>

scholarly journals Flavin-Tag: A Facile Method for Site-Specific Labeling of Proteins with a Flavin Fluorophore

2021 ◽  
Author(s):  
Yapei Tong ◽  
Misun Lee ◽  
Jeroen Drenth ◽  
Marco Fraaije
Keyword(s):  
Target Protein ◽  
Protein Labeling ◽  
Flexible Tool ◽  
Site Specific ◽  
Short Peptide

<p>Flavin-tag: we developed a facile method to label a target protein with a flavin. By using a short peptide (Flavin-tag), recognized by a flavinylating enzyme, FMN can be covalently incorporated. Attachment of the flavin chromo- and fluorophore can be performed <i>in vivo</i> and <i>in vitro</i> rendering the Flavin-tag a flexible tool for protein labeling.</p>

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

MEMORY EFFECTS IN THE FRAGMENTATION OF MOLECULES FOLLOWING SITE-SPECIFIC CORE EXCITATION

1987 ◽  
Vol 48 (C9) ◽  
pp. C9-741-C9-744 ◽  
Author(s):  
W. HABENICHT ◽  
L. A. CHEWTER ◽  
M. SANDER ◽  
K. MÜLLER-DETHLEFS ◽  
E. W. SCHLAG
Keyword(s):  
Memory Effects ◽  
Core Excitation ◽  
Site Specific
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