Conformational heterogeneity in linear peptides in solution: a carbon-1 3 NMR study of (Pro3, Pro5)-angiotensin-II.
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Amino Acids↗
Biomedical subjects
G C Levy
Publications and source records attributed to G C Levy.
Conformational flexibility of luteinizing hormone-releasing hormone in aqueous solution. A carbon-13 spin-lattice relaxation time study.
The carbon-13 nuclear magnetic resonance (13C NMR) spectra of luteinizing hormone-releasing hormone (LH-RH) and lower homologous peptides have been assigned in aqueous solutions at various pH values. 13C spin-lattice relaxation times (T1) have been measured for all proton-bearing carbons at 25.2 and 67.9 MHz. From the T1 data the rates of overall molecular motion and intramolecular motion of side chains have been estimated. LH-RH is a flexible molecule in solution, having segmental motion along the backbone as well as in the nonaromatic side chains.
Chemical Phenomena↗
High field carbon-13 NMR spectroscopy. Conformational mobility in gramicidin S and frequency dependence of 13-C spin-lattice relaxation times.
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Amino Acids↗
Carbon-13 nuclear magnetic resonance spectroscopy.
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Amino Acids↗
Planning and managing new and complex medical and surgical procedures.
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Computers↗