A global optimization method is described for identifying the global minimum energy conformation, as well as lower and upper bounds on the global minimum conformer of solvated peptides. In considering the effects of hydration, two independent continuum-based solvation models are employed. The first
The global minimum energy conformation of cyclotetraglycyl
โ Scribed by David N.J. White; Christopher Morrow
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- French
- Weight
- 226 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0040-4039
No coin nor oath required. For personal study only.
โฆ Synopsis
Cyclic peptides fulfil a diversity of biologically important functions by acting as hormones, toxins, antiobiotics, ion carriers, inhibitors etc. and in vivo activity is intimately related to their molecular conformations.
๐ SIMILAR VOLUMES
## Abstract The conformational energy of acetylcholine is minimized with respect to the distances between nonbonded atoms with the help of the Bremermann method of unconstrained global optimization. The set of distances for which the energy is the absolute minimum is then used to calculate the coor
## Abstract Based on the assumption that the conformational energy surface of a protein molecule can be approximated near the global minimum point by a multidimensional parabola, conformational fluctuations in the native state are discussed. In this approximation the conformational fluctuations can