Radical Anions of Cyclic Azoalkanes: An ESR, ENDOR, and TRIPLE-Resonance Study

1991 ◽  
Vol 74 (8) ◽  
pp. 2078-2093 ◽  
Author(s):  
Caspar H. Ess ◽  
Fabian Gerson ◽  
Waldemar Adam
Keyword(s):  
Radical Anions ◽  
Triple Resonance

ChemInform Abstract: Radical Anions of Cyclic Azoalkanes: An ESR, ENDOR, and TRIPLE- Resonance Study

ChemInform ◽  
2010 ◽  
Vol 23 (10) ◽  
pp. no-no
Author(s):  
C. H. ESS ◽  
F. GERSON ◽  
W. ADAM
Keyword(s):  
Radical Anions ◽  
Triple Resonance

ChemInform Abstract: Radical Anions of Cyclic Azoalkanes: An ESR, ENDOR, and TRIPLE- Resonance Study.

ChemInform ◽  
2010 ◽  
Vol 23 (18) ◽  
pp. no-no
Author(s):  
C. H. ESS ◽  
F. GERSON ◽  
W. ADAM
Keyword(s):  
Radical Anions ◽  
Triple Resonance

Radical Anions of Cyclic Azoalkanes: An ESR, ENDOR, and TRIPLE-Resonance Study

1992 ◽  
Vol 75 (1) ◽  
pp. 335-350 ◽  
Author(s):  
Caspar H. Ess ◽  
Fabian Gerson ◽  
Waldemar Adam
Keyword(s):  
Radical Anions ◽  
Triple Resonance

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.

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