title: Does a synthetic peptide containing the leucine-zipper domain of c-myb form an alpha-helical structure in solution?
abstract: We have examined a synthetic peptide containing the putative leucine zipper domain of the chicken c-myb proto-oncogene using circular dichroism (CD) spectroscopy. The peptide adopts an alpha-helical structure only at low temperatures and in the presence 2,2,2-trifluoroethanol.
authors.affiliation: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Ebneth
authors.forename: K
authors.initials: K
authors.lastname: Adermann
authors.forename: H
authors.initials: H
authors.lastname: Wolfes
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002942:Circular Dichroism; D003080:Cold Temperature; D006801:Humans; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins / Q000737:chemistry*; D020598:Proto-Oncogene Proteins c-myb; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D014270:Trifluoroethanol / Q000494:pharmacology
chemical_list: C000715470:MAS1 protein, human; D010446:Peptide Fragments; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins; D020598:Proto-Oncogene Proteins c-myb; D012996:Solutions; D014270:Trifluoroethanol