Identification of structured peptide segments in folding proteins.
Prediction of the structures of long polypeptides and small proteins has been carried out using conformational energy calculations. These calculations can be applied to large proteins if structured regions of their sequences can be identified. Three different approaches to identifying such sequences are presented. First, sequences of five or more contiguous hydrophobic residues tend to nucleate alpha-helices. Second, peptide sequences from parent proteins that have the same biological activities as the parent proteins are highly structured. Third, structured synthetic peptide segments from proteins inhibit the folding of the parent proteins by competing with the corresponding segment of the protein chain for associating with complementary regions. Examples of each of these approaches are presented.
Pincus
M R
MR
Department of Pathology, SUNY Health Science Center, Syracuse 13210.
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015717:Peptide T / Q000737:chemistry; D011487:Protein Conformation; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D012984:Software; D013816:Thermodynamics
D003574:Cytochrome c Group; D008565:Membrane Proteins; D015717:Peptide T; D012259:Ribonuclease, Pancreatic