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Comparison of conformational properties of proline and threonine residues

✍ Scribed by SIEMION, IGNACY Z. ;SOBCZYK, KATARZYNA ;LISOWSKI, MAREK

Book ID
115098444
Publisher
Wiley (Blackwell Publishing)
Year
2009
Tongue
English
Weight
651 KB
Volume
27
Category
Article
ISSN
0367-8377

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πŸ“œ SIMILAR VOLUMES

Conformations of proline residues in mem
Conformations of proline residues in membrane environments
✍ Charles M. Deber; Mira Glibowicka; G. Andrew Woolley πŸ“‚ Article πŸ“… 1990 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 799 KB

Although noted as hydrophilic residues with helix-breaking potential, proline residues are observed in putatively a-helical transmembrane (TM) segments of many channel-forming integral membrane proteins. In addition to the recognized property of X-Pro peptide bonds (where X = any amino acid) to occu

Chiroptical properties of S-proline conf
Chiroptical properties of S-proline conformational isomers
✍ F. S. Richardson; S. Ferber πŸ“‚ Article πŸ“… 1977 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 798 KB

## Abstract The chiroptical properties of S‐proline conformational isomers are examined on a theoretical model in which electronic wave functions are obtained from semiempirical molecular orbital calculations. The CNDO/S molecular orbital model is used to perform SCF‐MO calculations on ground state