The structural dependence of amino acid hydrophobicity parameters
โ Scribed by Marvin Charton; Barbara I. Charton
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 795 KB
- Volume
- 99
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
A statistical analysis was performed to determine to what extent an amino acid determines the identity of its neighbors and to what extent this is determined by the structural environment. Log-linear analysis was used to discriminate chance occurrence from statistically meaningful correlations. The
To better understand acyl transfer reactions of oligopeptides, seventeen N-acyl amino acid esters were solvolyzed in mildly basic methanol-d 4 . All show pseudo-first-order kinetics by 1 H NMR. The rate constant varies up to 400-fold with the identity of the amino acid and up to 6200-fold with the i
A two amino acid (hydrophobic and polar) scheme is used to perform the design on target conformations corresponding to the native states of 20 single chain proteins. Strikingly, the percentage of successful identification of the nature of the residues benchmarked against naturally occurring proteins