The enhanced role of a lanthanide shift reagent in the structure elucidation and1H NMR and13C NMR characterization of some marine natural products

1992 ◽  
Vol 3 (2) ◽  
pp. 73-79 ◽  
Author(s):  
Anthony D. Wright ◽  
Gabriele M. König ◽  
Otto Sticher
Keyword(s):  
Natural Products ◽  
Marine Natural Products ◽  
Structure Elucidation ◽  
Shift Reagent ◽  
Lanthanide Shift Reagent ◽  
Nmr Characterization

NMR characterization of complex natural products: Assigning novel, proton-deficient alkaloid scaffolds

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
KR Gustafson ◽  
STS Chan ◽  
D Milanowski
Keyword(s):  
Natural Products ◽  
Nmr Characterization

scholarly journals Evidence that the TRPV1 S1-S4 Membrane Domain Contributes to Thermosensing

2019 ◽  
Author(s):  
Minjoo Kim ◽  
Nicholas J. Sisco ◽  
Jacob K. Hilton ◽  
Camila M. Montano ◽  
Manuel A. Castro ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Solution Nmr ◽  
Membrane Domain ◽  
Temperature Dependent ◽  
Nmr Characterization ◽  
Significant Interest ◽  
Pore Domain ◽  
Coupling Mechanisms

AbstractSensing and responding to temperature is crucial in biology. The TRPV1 ion channel is a well-studied heat-sensing receptor that is also activated by vanilloid compounds including capsaicin. Despite significant interest, the molecular underpinnings of thermosensing have remained elusive. The TRPV1 S1-S4 membrane domain couples chemical ligand binding to the pore domain during channel gating. However, the role of the S1-S4 domain in thermosensing is unclear. Evaluation of the isolated human TRPV1 S1-S4 domain by solution NMR, Far-UV CD, and intrinsic fluorescence shows that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity. Further NMR characterization of the temperature-dependent conformational changes suggests the contribution of the S1-S4 domain to thermosensing shares features with known coupling mechanisms between this domain with ligand and pH activation. Taken together, this study shows that the TRPV1 S1-S4 domain contributes to TRPV1 temperature-dependent activation.

Characterization of apoptosis induced by marine natural products in non small cell lung cancer A549 cells

2006 ◽  
Vol 63 (19-20) ◽  
pp. 2377-2386 ◽  
Author(s):  
A. Catassi ◽  
A. Cesario ◽  
D. Arzani ◽  
P. Menichini ◽  
A. Alama ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Natural Products ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Marine Natural Products ◽  
A549 Cells ◽  
Small Cell ◽  
Small Cell Lung

scholarly journals NMR Characterization of the Interactions Between Glycosaminoglycans and Proteins

2021 ◽  
Vol 8 ◽  
Author(s):  
Changkai Bu ◽  
Lan Jin
Keyword(s):  
Protein Interactions ◽  
Dimensional Space ◽  
Three Dimensional ◽  
Gag Protein ◽  
Physiological Processes ◽  
Nmr Characterization ◽  
Mammalian Tissues ◽  
Three Dimensional Space

Glycosaminoglycans (GAGs) constitute a considerable fraction of the glycoconjugates found on cellular membranes and in the extracellular matrix of virtually all mammalian tissues. The essential role of GAG-protein interactions in the regulation of physiological processes has been recognized for decades. However, the underlying molecular basis of these interactions has only emerged since 1990s. The binding specificity of GAGs is encoded in their primary structures, but ultimately depends on how their functional groups are presented to a protein in the three-dimensional space. This review focuses on the application of NMR spectroscopy on the characterization of the GAG-protein interactions. Examples of interpretation of the complex mechanism and characterization of structural motifs involved in the GAG-protein interactions are given. Selected families of GAG-binding proteins investigated using NMR are also described.

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