title: Role of hydrophobic interactions in protein chain folding during biosynthesis.
abstract: It has been found that hydrophobic potentials of 30- to 40-amino acid fragments of amino acid sequences of myoglobin, cytochrome b5, alpha-chymotrypsin, and seven other globular proteins analyzed are similar and correspond to free energies of formation of limited hydrophobic nuclei.
authors.affiliation: Lviv Franko State University, Lviv, 290005, Ukraine.
authors.forename: A V
authors.initials: AV
authors.lastname: Trikulenko
mesh_terms: D002918:Chymotrypsin / Q000096:biosynthesis / Q000737:chemistry; D015786:Cytochromes b5 / Q000096:biosynthesis / Q000737:chemistry; D008956:Models, Chemical; D009211:Myoglobin / Q000096:biosynthesis / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D014176:Protein Biosynthesis; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D009211:Myoglobin; D010446:Peptide Fragments; D011506:Proteins; D015786:Cytochromes b5; D002918:Chymotrypsin