Conformational properties of pairs of amino acids.
Crystal structure data of 31 different globular proteins were analysed. Potentials for all 400 pairs of 20 amino acid residues in helix, extended structure, chain reversals and coil state were obtained. Analysis of these potentials showed that tripeptides of amino acid residues are not linear combinations of amino acids. The association effect of these tripeptides depends on the types of amino acids associated, the position of amino acids in the pair and the secondary structure in which the pair exists. This built-in information in tripeptides should be used in polypeptide and protein folding studies.
D000596:Amino Acids; D003461:Crystallography; D006860:Hydrogen Bonding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000596:Amino Acids