Analysis of helical structures of medium-sized polypeptides
โ Scribed by P. Amodeo; V. Barone; F. Fratenali
- Book ID
- 103637872
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 164 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0263-7855
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Abstract Single chain and packing energy calculations have been made on polyglycine (threefold and fourfold helical structures) with interchain NHโฆ๏ธO hydrogen bonds. In conformation __A__ of polyglycine, in which the NH groups point away from the helix axis and the CO groups are nearer to the he
## Abstract The sequential copolymers of glycine and Lโalanine, Lโvaline and Lโalanine, Lโleucine and Lโalanine, and Lโphenylalanine and Lโalanine and those containing the Lโproline residues were synthesized. The infrared spectra in the region from 700 to 200 cm^โ1^ were measured for these polypept
A study of the super helical structure of synthetic polypeptideb, such aa poly-7benzyl-r, (or L)-glutamate (PBDG or PBLG) waa carried out. The PBG waa dissolved in dimethylformamide (DMF). The solution waa either allowed to remain at room temperature for a long time or poured into some fatty acid, s
## Abstract An __ab initio__ method has been developed to predict helix formation for polypeptides. The approach relies on the systematic analysis of overlapping oligopeptides to determine the helical propensity for individual residues. Detailed atomistic level modeling, including entropic contribu