Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds

2017 ◽  
Vol 53 (99) ◽  
pp. 13205-13208 ◽  
Author(s):  
Michael D. Lee ◽  
Matthew L. Dennis ◽  
Bim Graham ◽  
James D. Swarbrick
Keyword(s):  
Nmr Spectroscopy ◽  
Paramagnetic Nmr ◽  
Nmr Studies ◽  
Lanthanide Binding Tags

A new pair of enantiomeric two-armed lanthanide-binding tags have been developed for paramagnetic NMR studies of proteins.

Enantiomeric two-armed lanthanide-binding tags for complementary effects in paramagnetic NMR spectroscopy

2016 ◽  
Vol 52 (51) ◽  
pp. 7954-7957 ◽  
Author(s):  
Michael D. Lee ◽  
Matthew L. Dennis ◽  
James D. Swarbrick ◽  
Bim Graham
Keyword(s):  
Nmr Spectroscopy ◽  
Paramagnetic Nmr ◽  
Lanthanide Binding Tags ◽  
Structural Restraints

A new pair of two-armed lanthanide-binding tags provide distinct sets of structural restraints when attached to the same site of a protein.

scholarly journals Compact, hydrophilic, lanthanide-binding tags for paramagnetic NMR spectroscopy

2015 ◽  
Vol 6 (4) ◽  
pp. 2614-2624 ◽  
Author(s):  
M. D. Lee ◽  
C.-T. Loh ◽  
J. Shin ◽  
S. Chhabra ◽  
M. L. Dennis ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Paramagnetic Nmr ◽  
Design Synthesis ◽  
Lanthanide Binding Tags

The design, synthesis and evaluation of four novel lanthanide-binding tags for paramagnetic NMR spectroscopy are reported.

NMR spectroscopy in the conformational analysis of peptides: an overview

2020 ◽  
Vol 27 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Interactions ◽  
3D Structure ◽  
Theoretical Background ◽  
Triple Resonance ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Conformational Preferences ◽  
Dynamic Perspective ◽  
Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

scholarly journals Comprehensive Characterisation of the Ketoprofen-β-Cyclodextrin Inclusion Complex Using X-ray Techniques and NMR Spectroscopy

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 4089
Author(s):  
Katarzyna Betlejewska-Kielak ◽  
Elżbieta Bednarek ◽  
Armand Budzianowski ◽  
Katarzyna Michalska ◽  
Jan K. Maurin
Keyword(s):  
Nmr Spectroscopy ◽  
Inclusion Complex ◽  
Crystal And Molecular Structure ◽  
Binding Constants ◽  
Nmr Studies ◽  
X Ray ◽  
Cyclodextrin Inclusion ◽  
Powder Samples ◽  
Cyclodextrin Inclusion Complex ◽  
Co Precipitation

Racemic ketoprofen (KP) and β-cyclodextrin (β-CD) powder samples from co-precipitation (1), evaporation (2), and heating-under-reflux (3) were analysed using X-ray techniques and nuclear magnetic resonance (NMR) spectroscopy. On the basis of NMR studies carried out in an aqueous solution, it was found that in the samples obtained by methods 1 and 2, there were large excesses of β-CD in relation to KP, 10 and 75 times, respectively, while the sample obtained by method 3 contained equimolar amounts of β-CD and KP. NMR results indicated that KP/β-CD inclusion complexes were formed and the estimated binding constants were approximately 2400 M−1, showing that KP is quite strongly associated with β-CD. On the other hand, the X-ray single-crystal technique in the solid state revealed that the (S)-KP/β-CD inclusion complex with a stoichiometry of 2:2 was obtained as a result of heating-under-reflux, for which the crystal and molecular structure were examined. Among the methods used for the preparation of the KP/β-CD complex, only method 3 is suitable.

Installation of a Rigid EDTA-Like Motif into a Protein α-Helix for Paramagnetic NMR Spectroscopy with Cobalt(II) Ions

2015 ◽  
Vol 22 (4) ◽  
pp. 1228-1232 ◽  
Author(s):  
James D. Swarbrick ◽  
Phuc Ung ◽  
Matthew L. Dennis ◽  
Michael D. Lee ◽  
Sandeep Chhabra ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Paramagnetic Nmr ◽  
Α Helix

Selectively Labeling the Heterologous Protein in Escherichia coli for NMR Studies: A Strategy to Speed Up NMR Spectroscopy

2001 ◽  
Vol 148 (1) ◽  
pp. 142-146 ◽  
Author(s):  
F.C.L. Almeida ◽  
G.C. Amorim ◽  
V.H. Moreau ◽  
V.O. Sousa ◽  
A.T. Creazola ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Heterologous Protein ◽  
Nmr Studies ◽  
Speed Up
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