Vijayan, M and Suresh, CG (1985) Head-to-tail sequences and other patterns of peptide aggregation in the solid state. In: International Journal of Peptide & Protein Research, 26 (3). pp. 311-328.
Full text not available from this repository. (Request a copy)Abstract
The available crystal structures of unprotected peptides were analyzed to investigate head-to-tail sequences and other patterns of peptide aggregation in the solid state. The no. of available dipeptide structures is large enough to permit meaningful conclusions. The dipeptide mols. in the crystal structures can be broadly classified as extended or folded, depending upon their conformations. The basic elements of dipeptide aggregation are different types of head-to-tail sequences and sequences involving H bonds with the peptide N atom as the donor, generated by periodic translations and 21 screw axes. By using these basic elements and the known geometrical preferences of H bonds, it is possible to construct several plausible idealized patterns, mostly 2-dimensional, of dipeptide aggregation for extended as well as folded mols. The patterns obsd. in crystal structures are in substantial agreement with these idealized patterns. Infinite H-bonded sequences of the type obsd. in dipeptide structures remain the basic elements of aggregation in the structure of larger peptides also. The present anal. shows that peptide aggregation in the solid state is controlled primarily by interactions involving main-chain atoms. Also, despite the increased mol. flexibility of peptides in comparison with amino acids and the presence of addnl. H-bonding groups in them, head-to-tail sequences remain the most important intrinsic feature not only of amino acid aggregation.
| Item Type: | Journal Article |
|---|---|
| Publication: | International Journal of Peptide & Protein Research |
| Publisher: | Munksgaard, Copenhagen |
| Additional Information: | Copyright of this article belongs to Munksgaard, Copenhagen. |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 08 Jul 2008 |
| Last Modified: | 27 Aug 2008 13:32 |
| URI: | http://eprints.iisc.ac.in/id/eprint/14755 |
Actions (login required)
 |
View Item |
