NMR Studies on hydrophobic interactions in solution Part 3 Salt effects on the self-association of ethanol in water at two different temperatures

1998 ◽  
Vol 94 (15) ◽  
pp. 2089-2092 ◽  
Author(s):  
Antonio Sacco ◽  
Francesca Maria De Cillis ◽  
Manfred Holz
Keyword(s):  
Hydrophobic Interactions ◽  
The Self ◽  
Nmr Studies ◽  
Salt Effects ◽  
Different Temperatures ◽  
Self Association ◽  
Ethanol In Water

The self-association of the cyclotide kalata B2 in solution is guided by hydrophobic interactions

Biopolymers ◽  
2013 ◽  
Vol 100 (5) ◽  
pp. 453-460 ◽  
Author(s):  
K. Johan Rosengren ◽  
Norelle L. Daly ◽  
Peta J. Harvey ◽  
David J. Craik
Keyword(s):  
Hydrophobic Interactions ◽  
The Self ◽  
Self Association

NMR Studies on the Self-Association of Uridine and Uridine Analogues

1998 ◽  
Vol 4 (4) ◽  
pp. 621-628 ◽  
Author(s):  
Anita Dunger ◽  
Hans-Heinrich Limbach ◽  
Klaus Weisz
Keyword(s):  
The Self ◽  
Nmr Studies ◽  
Self Association

scholarly journals Erratum: The self-association of the cyclotide kalata B2 in solution is guided by hydrophobic interactions

Biopolymers ◽  
2013 ◽  
Vol 102 (1) ◽  
pp. 136-136
Author(s):  
K. Johan Rosengren ◽  
Norelle L. Daly ◽  
Peta J. Harvey ◽  
David J. Craik
Keyword(s):  
Hydrophobic Interactions ◽  
The Self ◽  
Self Association

Hydrophobic Interactions in Solution: A Nuclear Magnetic Resonance Approach

2000 ◽  
Vol 214 (7) ◽  
Author(s):  
A. Sacco
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Hydrophobic Interactions ◽  
The Self ◽  
Aqueous Mixtures ◽  
Organic Components ◽  
Self Association ◽  
Small Hydrophobic ◽  
Nuclear Magnetic

The self-association behaviour of relatively small hydrophobic organic components in aqueous mixtures has been investigated by the application of an NMR technique. The association A

scholarly journals Preparation, structures and preliminary host–guest studies of fluorinated syn-bis-quinoxaline molecular tweezers

2010 ◽  
Vol 6 ◽  
Author(s):  
Markus Etzkorn ◽  
Jacob C Timmerman ◽  
Matthew D Brooker ◽  
Xin Yu ◽  
Michael Gerken
Keyword(s):  
Crystal Structure ◽  
Chemical Exchange ◽  
Solvent Molecule ◽  
The Self ◽  
Synthetic Route ◽  
Nmr Studies ◽  
Molecular Tweezers ◽  
Self Association ◽  
Molecular Tweezer ◽  
Bound Electron

A series of polycyclic frameworks with fluorinated syn-facial quinoxaline sidewalls has been prepared as potential molecular tweezers for electron-rich guest compounds. Our synthetic route to the cyclooctadiene-derived scaffolds 16a–d takes advantage of the facile isolation of a novel spirocyclic precursor 9b with the crucial syn-orientation of its two alkene moieties. The crystal structure of 16c displays two features typical of a molecular tweezer: inclusion of a solvent molecule in the molecular cleft and self-association of the self-complementary scaffolds. Furthermore, host–guest NMR studies of compound 16c in solution show chemical exchange between the unbound and bound electron-rich guest, N,N,N′,N′-tetramethyl-p-phenylenediamine.

1H and13C NMR studies on the self-association of retinoic acid

1990 ◽  
Vol 28 (3) ◽  
pp. 223-226 ◽  
Author(s):  
D. Vincent Waterhous ◽  
Donald D. Muccio
Keyword(s):  
Retinoic Acid ◽  
The Self ◽  
Nmr Studies ◽  
1H And13c Nmr ◽  
Self Association

scholarly journals The interplay of self-assembly and target binding in centrin 1 from Toxoplasma gondii

2021 ◽  
Author(s):  
Carolina Conter ◽  
Luca Bombardi ◽  
Marco Pedretti ◽  
Filippo Favretto ◽  
Adele Di Matteo ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Self Assembly ◽  
Metal Binding ◽  
Hydrophobic Interactions ◽  
Structural Features ◽  
The Self ◽  
Intact Protein ◽  
Titration Calorimetry ◽  
Self Association ◽  
Target Binding

Centrins are conserved calcium (Ca2+)-binding proteins typically associated with centrosomes that have been implicated in several biological processes. In Toxoplasma gondii, a parasite that causes toxoplasmosis, three centrin isoforms have been recognized. We have recently characterized the metal binding and structural features of isoform 1 (TgCEN1), demonstrating that it possesses properties consistent with a role as a Ca2+ sensor and displays a Ca2+-dependent tendency to self-assemble. Herein, we expanded our studies, focusing on the self-association and target binding properties of TgCEN1 by combining biophysical techniques including dynamic light scattering, isothermal titration calorimetry, nuclear magnetic resonance, circular dichroism, and fluorescence spectroscopy. We found that the self-assembly process of TgCEN1 depends on different physicochemical factors, including Ca2+ concentration, temperature, and protein concentration, and is mediated by both electrostatic and hydrophobic interactions. The process is completely abolished upon removal of the first 21-residues of the protein and is significantly reduced in the presence of a binding target peptide derived from the human XPC protein (P17-XPC). Titration of P17-XPC to the intact protein and isolated domains showed that TgCEN1 possesses two binding sites with distinct affinities and Ca2+ sensitivity; a high-affinity site in the C-lobe which may be constitutively bound to the peptide and a low-affinity site in the N-lobe which is active only upon Ca2+ stimulus. Overall, our results suggest a specific mechanism of TgCEN1 for Ca2+-modulated target binding and support a N-to-C self-assembly mode, in which the first 21-residues of one molecule likely interact with the C-lobe of the other.

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