Fourier transform-IR and 1 H NMR studies on the structure of water solubilized by reverse aggregates of calcium bis(2-ethylhexyl) sulfosuccinate in organic solvents

2000 ◽  
Vol 278 (2) ◽  
pp. 143-149 ◽  
Author(s):  
O.A. El Seoud ◽  
L. P. Novaki ◽  
P. A. R. Pires
Keyword(s):  
Fourier Transform ◽  
Organic Solvents ◽  
Nmr Studies ◽  
Structure Of Water ◽  
H Nmr ◽  
Fourier Transform Ir

N-Confused porphyrins: complexation and 1H NMR studies

2017 ◽  
Vol 41 (16) ◽  
pp. 7932-7937 ◽  
Author(s):  
Ilya A. Khodov ◽  
Olga V. Maltceva ◽  
Vladimir V. Klochkov ◽  
Oscar I. Koifman ◽  
Nugzar Zh. Mamardashvili
Keyword(s):  
Organic Solvents ◽  
1H Nmr ◽  
Nmr Studies ◽  
H Nmr ◽  
Vis Spectroscopy

The complexation of 2-aza-21-carba-tetraphenylporphyrin and 2-aza-2-methyl-5,10,15,20-tetraphenyl-21-carbaporphyrin with nickel and zinc acetates in organic solvents has been investigated by UV-Vis spectroscopy and 1H NMR.

scholarly journals Two-dimensional Fourier transform 1 H NMR studies of ribosomal protein E-L30

FEBS Letters ◽  
1984 ◽  
Vol 169 (1) ◽  
pp. 107-111 ◽  
Author(s):  
F.J.M. van de Ven ◽  
S.H. de Bruin ◽  
C.W. Hilbers
Keyword(s):  
Fourier Transform ◽  
Ribosomal Protein ◽  
Two Dimensional ◽  
Nmr Studies ◽  
H Nmr

Fourier transform IR monitoring of porous silicon passivation during post-treatments such as anodic oxidation and contact with organic solvents

1995 ◽  
Vol 255 (1-2) ◽  
pp. 200-203 ◽  
Author(s):  
M.A. Hory ◽  
R. Hérino ◽  
M. Ligeon ◽  
F. Muller ◽  
F. Gaspard ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Porous Silicon ◽  
Organic Solvents ◽  
Anodic Oxidation ◽  
Fourier Transform Ir

ChemInform Abstract: FOURIER TRANSFORM IR AND NMR STUDIES OF HYDROGEN BONDING IN HELMINTHOSPORIUM CARBONUM TOXIN

1984 ◽  
Vol 15 (40) ◽  
Author(s):  
M. POPE ◽  
P. MASCAGNI ◽  
W. A. GIBBONS ◽  
L. M. CIUFFETTI ◽  
H. W. KNOCHE
Keyword(s):  
Hydrogen Bonding ◽  
Fourier Transform ◽  
Nmr Studies ◽  
Fourier Transform Ir

Fourier transform IR and NMR studies of hydrogen bonding in Helminthosporium carbonum toxin

1984 ◽  
Vol 106 (13) ◽  
pp. 3863-3865 ◽  
Author(s):  
Mark Pope ◽  
Paolo Mascagni ◽  
William A. Gibbons ◽  
Lynda M. Ciuffetti ◽  
Herman W. Knoche
Keyword(s):  
Hydrogen Bonding ◽  
Fourier Transform ◽  
Nmr Studies ◽  
Fourier Transform Ir

1H NMR Conformational Studies in Water of Angiotensin II Analogues Modified at the N- and C-Termini: Interactions of the Aromatic Side Chains and Folding of the N-Terminal Domain

1994 ◽  
Vol 59 (11) ◽  
pp. 2523-2532 ◽  
Author(s):  
John Hondrelis ◽  
John Matsoukas ◽  
George Agelis ◽  
Paul Cordopatis ◽  
Ning Zhou ◽  
...  
Keyword(s):  
Shielding Effect ◽  
Resonance Spectroscopy ◽  
Nmr Studies ◽  
Previous Suggestion ◽  
Aminoisobutyric Acid ◽  
H Nmr ◽  
Neutral Ph ◽  
Angiotensin Ii Analogues ◽  
Proton Resonances ◽  
Cosy Nmr

The conformation of [Sar1]angiotensin II in water at neutral pH has been examined by proton magnetic resonance spectroscopy at 400 MHz and in particular by comparing its 1H NMR spectral data with those of analogues modified at positions 1,4 and 6, namely [Sar1,Cha8]ANGII, [Des Asp1,Cha8]ANGII, [Aib1,Tyr(Me)4]ANGII, [Aib1,Tyr(Me)4,Ile8]ANGII, [N-MeAib1,Tyr(Me)4]ANGII, [N-MeAib1,Tyr(Me)4,Ile8]ANGII, ANGIII and [Sar1,Ile8]ANGII. Assignment of all proton resonances in these analogues was made possible by 2D COSY NMR experiments. The H-2 and H-4 protons for the histidine ring in [Sar1]ANGII, ANGII and ANGIII were shielded compared with the same protons in [Sar1,Ile8]ANGII, [Sar1,Cha8]ANGII and [Des Asp1,Cha8]ANGII; this shielding effect was not disturbed upon methylation of the tyrosine hydroxyl and/or replacement of residue 1 (sarcosine or aspartic acid) with aminoisobutyric acid (Aib) or N-methyl aminoisobutyric acid (N-MeAib). These data are consistent with our previous suggestion based on NMR studies in neutral DMSO that a characteristic folded conformation for ANGII previously observed in non-polar solvents can also be detected in water at neutral pH, but to a lesser degree.

Sign in / Sign up

Export Citation Format

Share Document