Improved Resolution and Sensitivity of Triple-Resonance NMR Methods for the Structural Analysis of Proteins by Use of a Backbone-Labeling Strategy

1999 ◽  
Vol 121 (50) ◽  
pp. 11871-11874 ◽  
Author(s):  
Philip E. Coughlin ◽  
Frank E. Anderson ◽  
Ed J. Oliver ◽  
Jonathan M. Brown ◽  
Steve W. Homans ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Nmr Methods

Double and Triple Resonance NMR Methods for Protein Assignment

2003 ◽  
pp. 29-52 ◽  
Author(s):  
Brian Whitehead ◽  
C. Jeremy Craven ◽  
Jonathan P. Waltho
Keyword(s):  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Protein Assignment ◽  
Nmr Methods

Applications of1H—19F—13C Triple-Resonance NMR Methods to the Characterization of Fluoropolymers

1995 ◽  
pp. 215-242 ◽  
Author(s):  
Peter L. Rinaldi ◽  
Lan Li ◽  
Dale G. Ray ◽  
Gerard S. Hatvany ◽  
Hsin-Ta Wang ◽  
...  
Keyword(s):  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Nmr Methods

Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins

1992 ◽  
Vol 114 (6) ◽  
pp. 2262-2264 ◽  
Author(s):  
Wayne Boucher ◽  
Ernest D. Laue ◽  
Sharon Campbell-Burk ◽  
Peter J. Domaille
Keyword(s):  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Nmr Methods

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 Phage display-derived ligands provide structural insight into insulin-like growth factor I function

2004 ◽  
Vol 18 (2) ◽  
pp. 237-249
Author(s):  
Nicholas J. Skelton ◽  
Michelle L. Schaffer ◽  
Kurt Deshayes ◽  
Tamas Blandl ◽  
Steven Runyon ◽  
...  
Keyword(s):  
Growth Factor ◽  
Phage Display ◽  
Binding Proteins ◽  
Cell Surface Receptor ◽  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Growth Factor I

Insulin–like growth factor–I (IGF–I) is a central mediator of cell growth, differentiation and metabolism. Structural characterization of the protein has been hampered by a combination of internal dynamics and self–association that prevent crystallization and produce broad NMR resonances. To better characterize the functions of IGF–I, we have used phage display to identify peptides that antagonize the binding of IGF–I to its plasma binding proteins (IGFBPs) and cell–surface receptor (IGF–R). Interestingly, binding of peptide improves dramatically the quality of the NMR resonances of IGF–I, and enables the use of triple–resonance NMR methods to characterize the complexes. One such peptide, designated IGF–F1–1, has been studied in detail. In the complex, the peptide retains the same loop–helix motif seen in the free state whilst IGF–I contains three helices, as has been seen previously in low–resolution structures in the absence of ligand. The peptide binds at a hydrophobic patch between helix 1 and 3, a site identified previously by mutagenesis as a contact site for IGFBP1. Thus, antagonism of IGFBP1 binding exhibited by the peptide occurs by a simple steric occlusion mechanism. Antagonism of IGF–R binding may also be explained by a similar mechanism if receptor binding occurs by a two–site process, as has been postulated for insulin binding to its receptor. Comparisons with crystallographic structures determined for IGF–I in other complexes suggest that the region around helix 1 of IGF–I is conformationally conserved whereas the region around helix 3 adopts several different ligand–induced conformations. The ligand–induced structural variability of helix 3 appears to be a common feature across the insulin super–family. In the case of IGF–I, exchange between such conformations may be the source of the dynamic nature of free IGF–I, and likely has functional significance for the ability of IGF–I to recognize two signaling receptors and six binding proteins with high affinity.

Co-polymerization analysis of thermosetting resins using1H-15N-13C triple resonance NMR spectroscopy

2012 ◽  
Vol 128 (5) ◽  
pp. 3375-3381 ◽  
Author(s):  
Amy Philbrook ◽  
Scott Earnshaw ◽  
Christopher J. Easton ◽  
Max A. Keniry ◽  
Melissa J. Latter
Keyword(s):  
Nmr Spectroscopy ◽  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Thermosetting Resins ◽  
Triple Resonance Nmr Spectroscopy
Sign in / Sign up

Export Citation Format

Share Document