The specific concentration dependence of the proton magnetic resonance chemical shift in the system acetic acid–water

1981 ◽  
Vol 74 (11) ◽  
pp. 6532-6533 ◽  
Author(s):  
L. Kimtys ◽  
V. Balevičius
2007 ◽  
Vol 111 (31) ◽  
pp. 9270-9280 ◽  
Author(s):  
Toshiyuki Takamuku ◽  
Yasuhiro Kyoshoin ◽  
Hiroshi Noguchi ◽  
Shoji Kusano ◽  
Toshio Yamaguchi

1965 ◽  
Vol 43 (11) ◽  
pp. 3057-3062 ◽  
Author(s):  
Natsuko Cyr ◽  
Leonard W. Reeves

The keto–enol equilibrium of cyclohexane-1,3-dione in chloroform is best interpreted from proton resonance measurements as[Formula: see text]K1 and K2 may be separately determined from chemical shift measurements of the enol-OH proton and intensity measurements of peaks assigned to keto and enol forms. K1 and K2 are satisfactorily independent of concentrations except in very dilute solutions where intensity measurements become unreliable. The overall equilibrium constant K = K1 × K22 can be obtained for the same molecule in acetonitrile solutions where the enol monomer form is in very low concentration. 5,5′-Dimethylcyclohexane-1,3-dione in chloroform has less enol form than the unsubstituted molecule. The enthalpy change associated with 'K' for cyclohexane-1,3-dione in chloroform is 2.05 ± 0.5 kcal mole−1.


2011 ◽  
Vol 51 (5) ◽  
pp. 819-825 ◽  
Author(s):  
Housheng Hong ◽  
Longxiang Chen ◽  
Qingwen Zhang ◽  
Zheran Zhang

1974 ◽  
Vol 52 (11) ◽  
pp. 1013-1017 ◽  
Author(s):  
William H. Cruickshank ◽  
Barry L. Malchy ◽  
Harvey Kaplan

Thiolysis of an O-dinitrophenyl-tyrosyl peptide results in an increased solubility in the stationary phase of a n-butanol – acetic acid – water – pyridine (15:3:12:10) (BAWP) paper chromatographic system. It is shown that this property can be used to form the basis of a diagonal paper chromatographic purification of tyrosyl peptides from enzymatic digests of proteins. The amino groups of the protein are first reacted with citraconic anhydride and then the citraconyl protein is reacted with 1-fluoro-2,4-dinitrobenzene. The dinitrophenyl-citraconyl protein is subjected to enzymatic digestion, applied to a strip of Whatman 3 MM paper, thiolyzed with 5% 2-mercaptoethanol in acetone, and subjected to chromatography using BAWP as solvent. A guide strip is removed, thiolyzed with 5% 2-mercaptoethanol in 25% pyridine, and resubjected to chromatography in BAWP at right angles to the original direction of chromatography. The tyrosyl peptides are displaced off the diagonal towards the origin. The off-diagonal peptides are isolated from the original chromatogram by thiolysis and chromatography using the diagonal chromatogram to locate the positions of the dinitrophenyl-tyrosyl peptides.


Sign in / Sign up

Export Citation Format

Share Document