title: The formation of protein secondary structure. Its connection with amino acid sequence.
abstract: Statistical analysis of the occurrence of tetrapeptides in 35 globular proteins was performed. It was found that the amino acids along the polypeptide chain are close to being randomly distributed and that the same tetrapeptide segments exist in different types of secondary structure. Therefore, a new method was proposed for locating 'microdomains' in protein interiors. Amino acid replacements in the hydrophobic core of six proteins were analyzed. The results show that the locations of amino acids belonging to defined microdomains are extremely conserved. It is suggested that the structures found may play a role as nucleation centers in protein folding.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
authors.forename: P
authors.initials: P
authors.lastname: Zielenkiewicz
authors.forename: D
authors.initials: D
authors.lastname: Płochocka
authors.forename: A
authors.initials: A
authors.lastname: Rabczenko
mesh_terms: D000595:Amino Acid Sequence; D008962:Models, Theoretical; D011487:Protein Conformation; D011506:Proteins; D012259:Ribonuclease, Pancreatic
chemical_list: D011506:Proteins; D012259:Ribonuclease, Pancreatic