Conformational analysis of melittin using the residual representation
β Scribed by Bernard Busetta
- Book ID
- 115911405
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 289 KB
- Volume
- 117
- Category
- Article
- ISSN
- 0014-5793
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π SIMILAR VOLUMES
The conformational space of the 20-residue membrane-bound portion of melittin has been investigated extensively with the conformational space annealing (CSA) method and the ECEPP/3 (Empirical Conformational Energy Program for Peptides) algorithm. Starting from random conformations, the CSA method fi
## Abstract The vibrational absorption and vibrational circular dichroism (VCD) spectra of melittin in D~2~O solutions at different pH values, different salt concentrations, or different 2,2,2βtrifluoroethanol (TFE) concentrations are recorded in the amide Iβ² (1850β1600 cm^β1^) region. Two models a
A successful implementation of a parallel version of a conformational Ε½ . space annealing CSA method is presented. The CSA method, an optimization procedure for conformational energy calculations on polypeptides, searches the whole conformational space in its early stages and then narrows the search