Peptide Conformations. I. Nuclear Magnetic Resonance Study of the Carbamate Reaction of Amino Acids and Peptides

1971 ◽  
Vol 49 (5) ◽  
pp. 767-776 ◽  
Author(s):  
R. U. Lemieux ◽  
M. A. Barton
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Nuclear Magnetic Resonance Study ◽  
Amide Bond ◽  
Resonance Spectroscopy ◽  
Peptide Conformations ◽  
End Distance ◽  
Phenylalanine Residue ◽  
Nuclear Magnetic

Nuclear magnetic resonance spectroscopy has been applied to the study of carbamate formation in solutions of amino acids and peptides in a carbonate-bicarbonate system. The possible conformations of these carbamates are discussed in terms of the n.m.r. data obtained. The n.m.r. parameters are reported for the diastereomers L-alanyl-L or D-phenylalanine and L-phenylalanyl-L or D-alanine and for the dipeptide glycyl-L-phenylalanine and their carbamates. The results are interpreted in terms of preferred rotamers about the Cα—Cβ bond of the phenylalanine residue and a β-type conformation of the peptide chain, wherein the two α-protons lie in the plane of the amide bond. All observations are in agreement with a shorter end to end distance in L,D- compared with L,L-dipeptides.

A Nuclear Magnetic Resonance Study of the Metal Binding Sites in Bacitracin

1975 ◽  
Vol 53 (12) ◽  
pp. 1250-1254 ◽  
Author(s):  
Roderick E. Wasylishen ◽  
Moira R. Graham
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Binding ◽  
Binding Sites ◽  
Imidazole Ring ◽  
Nuclear Magnetic Resonance Study ◽  
Resonance Spectroscopy ◽  
Metal Binding Sites ◽  
Ph Values ◽  
Nuclear Magnetic

Carbon-13 nuclear magnetic resonance spectroscopy has been used to identify sites in bacitracin which bind Cu2+ and Mn2+. Results are presented which implicate the free carboxyl groups of the aspartic and glutamic acid residues and the imidazole ring of the histidine residue as metal complexation sites between pH 6 and 8. Evidence is presented which also indicates that the thiazoline ring of bacitracin binds Mn2+. Bacitracin does not bind Cu2+ or Mn2+ at pH values of 2.5 or less.

A 13C comparative nuclear magnetic resonance study of organic solute production and excretion by the yeasts Hansenula anomala and Saccharomyces cerevisiae in saline media

1988 ◽  
Vol 34 (5) ◽  
pp. 605-612 ◽  
Author(s):  
Yves Bellinger ◽  
François Larher
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Specific Property ◽  
Glucose Consumption ◽  
Nuclear Magnetic Resonance Study ◽  
Resonance Spectroscopy ◽  
Hansenula Anomala ◽  
Organic Solute ◽  
Nuclear Magnetic

Glycerol, arabitol and trehalose were the principle solutes detected in cellular extracts of Hansenula anomala, using natural-abundance 13C nuclear magnetic resonance spectroscopy. Only the two polyols accumulated in response to increased salinity, glycerol increase being far greater. Arabitol content also increased with culture age, independently of the presence or absence of salt and in line with the evolution of trehalose content. Glycerol retention potential was 15 times greater for Hansenula than for Saccharomyces cerevisiae. The former displayed the specific property of increasing this capacity in high salt concentrations. Under such conditions its growth was associated with a limited increase in glucose consumption per unit biomass, relative to S. cerevisiae, the salt-sensitive reference yeast. In addition, a polysaccharide, the chemical nature of which was not further characterized, was detected exclusively in the external medium of Hansenula growing in the presence of salt.

scholarly journals Metabolism of Lactate in Cultured GABAergic Neurons Studied by 13C Nuclear Magnetic Resonance Spectroscopy

1998 ◽  
Vol 18 (1) ◽  
pp. 109-117 ◽  
Author(s):  
Helle S. Waagepetersen ◽  
Inger J. Bakken ◽  
Orla M. Larsson ◽  
Ursala Sonnewald ◽  
Arne Schousboe
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Resonance Spectroscopy ◽  
Acid Cycle ◽  
Cell Extracts ◽  
Gaba Synthesis ◽  
Nuclear Magnetic

Primary cultures of mouse cerebral cortical neurons (GABAergic) were incubated for 4 hours in media without glucose containing 1.0 mmol/L [U-13C]lactate in the absence or presence of 0.5 mmol/L glutamine. Redissolved, lyophilized cell extracts were analyzed by 13C nuclear magnetic resonance spectroscopy to investigate neuronal metabolism of lactate and by HPLC for determination of the total amounts of glutamate (Glu), γ-aminobutyric acid (GABA), and aspartate (Asp). The 13C nuclear magnetic resonance spectra of cell extracts exhibited multiplets for Glu, GABA, and Asp, indicating pronounced recycling of labeled tricarboxylic acid cycle constituents. There was extensive incorporation of 13C label into amino acids in neurons incubated without glutamine, with the percent enrichments being approximately 60% for Glu and Asp, and 27% for GABA. When 0.5 mmol/L glutamine was added to the incubation medium, the enrichments for Asp, Glu, and GABA were 25%, 35%, and 25%, respectively. This strongly suggests that glutamine is readily converted to Glu and Asp but that conversion to GABA may be complex. The observation that enrichment in GABA was identical in the absence and presence of glutamine whereas cycling was decreased in the presence of glutamine indicates that only C-2 units derived from glutamine are used for GABA synthesis, that is, that metabolism through the tricarboxylic acid cycle is a prerequisite for GABA synthesis from glutamine. The current study gives further support to the hypothesis that cellular metabolism is compartmentalized and that lactate is an important fuel for neurons in terms of energy metabolism and extensively labels amino acids synthesized from tricarboxylic acid cycle intermediates (Asp and Glu) as well as the neurotransmitter in these neurons (GABA).

A 13C nuclear magnetic resonance study of selectivity in the binding of univalent counterions by heparin

1988 ◽  
Vol 66 (10) ◽  
pp. 2601-2604 ◽  
Author(s):  
Photis Dais ◽  
Kevin R. Holme ◽  
Arthur S. Perlin
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Nuclear Magnetic Resonance Study ◽  
Resonance Spectroscopy ◽  
Free Energies ◽  
Binding Selectivity ◽  
Hydrated Ions ◽  
Binding Preference ◽  
13C Nuclear Magnetic Resonance ◽  
Nuclear Magnetic

The binding selectivities of univalent counterions for heparin in the systems Ca2+/M+/HEP, where M+ = Li+, Na+, K+, Cs+, TMA+, have been studied by 13C nuclear magnetic resonance spectroscopy. Chemical shift displacements of the various 13C nuclei of heparin in these systems clearly indicate that the binding selectivity of the polymer for univalent counterions increases with an increase in the radius of the hydrated cation form, namely Li+ > Na+ > K+ > Cs+ > TMA+. An explanation for this binding preference is offered on the basis of electrostatic and entropic terms, whereby the latter is reflected in changes in the hydration volumes of the univalent cations. Differences in the magnitude of these hydration volumes, in relation to the free energies of hydration, may account for a binding selectivity that favours the more highly hydrated ions.

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