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Nonbonded interactions in membrane-active cyclic biopolymers. III. Analogs of valinomycin

✍ Scribed by K. Sundaram; R. S. Tyagi

Publisher
John Wiley and Sons
Year
1979
Tongue
English
Weight
302 KB
Volume
15
Category
Article
ISSN
0020-7608

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✦ Synopsis

Abstract

Several analogs of valinomycin have been simulated. These are analogs obtained by changing the configuration of the amino acid and hydroxy acid residues one at a time. Nonbonded interactions have been calculated for three conformations of each analog. The electrostatic and polarization contributions to the energy are conformation selective, whereas the Pauli repulsion is the only component which is isomer selective. For the ring chirality considered here the analog of valinomycin having all the three L‐valyl residues replaced by D‐valyl residues is predicted to be frozen in a β€œtop open” conformation.

πŸ“œ SIMILAR VOLUMES

Nonbonded interactions in membrane activ
Nonbonded interactions in membrane active cyclic biopolymers. II. Ion binding by valinomycin
✍ K. Sundaram; R. S. Tyagi πŸ“‚ Article πŸ“… 1978 πŸ› John Wiley and Sons 🌐 English βš– 493 KB

## Abstract A possible mode for the capture of a cation by the carrier molecule valinomycin has been simulated. The intramolecular nonbonded energy and the binding energy for a centrally located potassium ion at different stages in the capture process have been evaluated using a method proposed ear