ArticleBiophysical reviews2012
The spin label amino acid TOAC and its uses in studies of peptides: chemical, physicochemical, spectroscopic, and conformational aspects.
Article in Biophysical reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 73 citations in OpenAlex.
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- Synthesis, Conformational Analysis and Antitumor Activity of the Naturally Occurring Antimicrobial Medium-Length Peptaibol Pentadecaibin and Spin-Labeled Analogs Thereof.International journal of molecular sciences · 2023Article
- Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy.Bioconjugate chemistry · 2023Article
- Different Biophysical Properties of Cell Surface α2,3- and α2,6-Sialoglycans Revealed by Electron Paramagnetic Resonance Spectroscopic Studies.The journal of physical chemistry. B · 2023Article
- Is Cys(MTSL) the Best α-Amino Acid Residue to Electron Spin Labeling of Synthetically Accessible Peptide Molecules with Nitroxides?ACS omega · 2022Article
- Half a century deciphering membrane structure, dynamics and function: a short description of the life and research of Shirley Schreier.Biophysical reviews · 2021Article
- Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels.European biophysics journal : EBJ · 2021Review
- Light-Emitting Probes for Labeling Peptides.Cell reports. Physical science · 2020Article
- A Global Minimization Toolkit for Batch-Fitting and χBiophysical journal · 2020Article
- Conformational Dynamics in Extended RGD-Containing Peptides.Biomacromolecules · 2020Article
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins.Biomolecules · 2020Review
- Quantifying residue-specific conformational dynamics of a highly reactive 29-mer peptide.Scientific reports · 2020Article
- Trajectory-Based Simulation of EPR Spectra: Models of Rotational Motion for Spin Labels on Proteins.The journal of physical chemistry. B · 2019Article
- Article
- Site-Directed Spin Labeling EPR for Studying Membrane Proteins.BioMed research international · 2018Review
- New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.Archives of biochemistry and biophysics · 2017Review
- A Bifunctional Spin Label for Ligand Recognition on Surfaces.Angewandte Chemie (International ed. in English) · 2017Article
- Pulse EPR Measurements of Intramolecular Distances in a TOPP-Labeled Transmembrane Peptide in Lipids.Biophysical journal · 2016Article
- Calcium-Dependent Structural Dynamics of a Spin-Labeled RyR Peptide Bound to Calmodulin.Biophysical journal · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We review work on the paramagnetic amino acid 2,2,6,6-tetramethyl-N-oxyl-4-amino-4-carboxylic acid, TOAC, and its applications in studies of peptides and peptide synthesis. TOAC was the first spin label probe incorporated in peptides by means of a peptide bond. In view of the rigid character of this cyclic molecule and its attachment to the peptide backbone via a peptide bond, TOAC incorporation has been very useful to analyze backbone dynamics and peptide secondary structure. Many of these studies were performed making use of EPR spectroscopy, but other physical techniques, such as X-ray crystallography, CD, fluorescence, NMR, and FT-IR, have been employed. The use of double-labeled synthetic peptides has allowed the investigation of their secondary structure. A large number of studies have focused on the interaction of peptides, both synthetic and biologically active, with membranes. In the latter case, work has been reported on ligands and fragments of GPCR, host defense peptides, phospholamban, and β-amyloid. EPR studies of macroscopically aligned samples have provided information on the orientation of peptides in membranes. More recent studies have focused on peptide-protein and peptide-nucleic acid interactions. Moreover, TOAC has been shown to be a valuable probe for paramagnetic relaxation enhancement NMR studies of the interaction of labeled peptides with proteins. The growth of the number of TOAC-related publications suggests that this unnatural amino acid will find increasing applications in the future.
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