Conformational interpretation of intramolecular electron transfer in Met5-enkephalins between Tyr and Met(S:.Br) radical.

Mean distances between C beta atoms of redox centers and mean values of the exponentially distance dependent rate constants for intramolecular electron transfer, (k), in aqueous solution were calculated for Met5-enkephalin and its D-Ala2 analogue using the molecular mechanics and Monte Carlo techniques. The ratio of (k) values thus obtained proved similar to that determined experimentally for intramolecular electron transfer accompanying Met(S:.Br)----TyrO.

Dynamic space structure of the Leu-enkephalin molecule in DMSO solution.

The dynamical space structure of the Leu-enkephalin molecule in DMSO solution was described combining the ROE measurements and Monte Carlo energy calculations. The statistical weights for possible Leu-enkephalin conformers were estimated by comparing the NMR-experimental parameters and the same parameters average over statistical samples of molecular structures obtained by Monte Carlo techniques for every low-energy conformer. The statistical weight estimations reveal that the Leu-enkephalin molecule in DMSO solution is apparently represented by a mixture of at least two peptide backbone conformers with the mean statistical weight values of 70% and 30%.

[Spatial structure of angiotensin in an aqueous solution].

The spatial structure of spin-labeled angiotensin in aqueous solution wa investigated with the combined use of NMR, fluorescence spectroscopy and energy calculation including Monte-Carlo techniques. The calculated mean values of molecular parameters were compared with the experimental ones. The calculated and experimental mean values were regarded as statistically indistinguishable when the corresponding mean values occurred within the 95% confidence limit.

Combined use of spectroscopic and energy calculation methods for the determination of peptide conformation in solution.

This paper describes the combined use of energy calculations and spectroscopic data for the determination of peptide conformations in solution. The approach involves (i) experimental measurements of spectroscopic parameters for a molecule, (ii) calculation of these parameters for low-energy conformers previously determined with regard to local fluctuations in conformation and (iii) a random search for statistically weighted combinations of conformers which provide a good agreement between the calculated and experimental data. The above approach was used to study the conformation of a spin-labelled angiotensin molecule (SL-AT).

[Synthesis, biological activity and conformation of enkephalin analogs structurally related to kyotorphin].

[D-Arg2,Leu5]Enkephalin and two series of its N-terminal short-chain analogues with a free and modified C-terminal carboxylic group, viz. amides and ethyl esters of tri- and tetrapeptides, were synthesized in solution and by solid-phase method. Their analgesic activity, assayed by the "tail pinch" method following intracisternal and intravenous administration to mice, was compared with activity of enkephalins and morphine.