Detail of "7376-90-1"

Reference

Aqueous solutions containing amino acids and peptides

Aqueous solutions containing amino acids and peptides. Part 18. The enthalpy of solution of N-acetyl-L-phenylalaninamide in aqueous solutions containing formamide. Nelander, K.; Olofsson, G.; Blackburn, G. M.; Kent, H. E.; Lilley, T. H. (Thermochem. Chem. Cent., Univ. Lund, Lund S-220 07/7, Swed.). Thermochim. Acta, 78(1-3), 303-7 (English) 1984. CODEN: THACAS. ISSN: 0040-6031. DOCUMENT TYPE: Journal CA Section: 69 (Thermodynamics, Thermochemistry, and Thermal Properties) Section cross-reference(s): 68 The heats of soln. were detd. at 298.15 K of N-acetyl-L-phenylalaninamide (F) [7376-90-1] in water and aq. solns. contg. formamide (f). The data were treated to obtain the heterotactic pairwise interaction coeff. for F with f. The result disagrees with the value predicted by a group additivity approach and reasons for this discrepancy are suggested.

Intrinsic Folding of Small Peptide Chains: Spectroscopic Evidence for the Formation of b-Turns in the Gas Phase

Intrinsic Folding of Small Peptide Chains: Spectroscopic Evidence for the Formation of b-Turns in the Gas Phase.In this study， 7376-90-1 and 34017-16-8 are also used. Chin, Wutharath; Dognon, Jean-Pierre; Piuzzi, Francois; Tardivel, Benjamin; Dimicoli, Iliana; Mons, Michel (Laboratoire Francis Perrin (URA CEA-CNRS 2453) Service des Photons, Atomes et Molecules, Centre d'Etudes de Saclay, Gif-sur-Yvette 91191, Fr.). Journal of the American Chemical Society, 127(2), 707-712 (English) 2005 American Chemical Society. CODEN: JACSAT. ISSN: 0002-7863. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Laser desorption of model peptides coupled to laser spectroscopic techniques enables the gas-phase observation of genuine secondary structures of biol. Spectroscopic evidence for the formation of b-turns in gas-phase peptide chains contg. glycine and phenylalanine residues establishes the intrinsic stability of these forms and their ability to compete with other stable structures. The precise characterization of local min. on the potential energy surface from IR spectroscopy constitutes an acute assessment for the state-of-the-art quantum mech. calcns. also presented. The observation of different types of b-turns depending upon the residue order within the sequence is found to be consistent with the residue propensities in b-turns of proteins, which suggests that the prevalence of glycine in type II and II' turns stems essentially from an energetic origin, already at play under isolated conditions. .