title: Characterization of secondary structure of neocarzinostatin apoprotein.
abstract: Characteristics of the secondary structure of neocarzinostatin apoprotein (apo-NCS) were examined by various means. Gaussian analysis of the Fourier-transform infrared (FT-IR) curve and curve-fitting of the circular dichroism (CD) spectrum for apo-NCS revealed that this peptide was abundant in beta-structures. In the presence of sodium dodecyl sulfate (SDS), the CD bands of NCS originating from phenylalanyl, tyrosyl, and cystinyl residues decreased, indicating a conformational change around the chromophore (CNS-chr). On the other hand, apo-NCS, in the SDS system, showed no change of these bands. We showed that the major parts of the protein moiety consist of beta-structures by measurements of the FT-IR and CD spectra of apo-NCS and a prediction of the secondary structure based on the amino acid sequence of the peptide. It seems that properties of the protein may be important to the hydrophobic interaction between NCS-chr and apo-NCS.
authors.forename: K
authors.initials: K
authors.lastname: Saito
authors.forename: Y
authors.initials: Y
authors.lastname: Sato
authors.forename: K
authors.initials: K
authors.lastname: Edo
authors.forename: Y
authors.initials: Y
authors.lastname: Akiyama-Murai
authors.forename: Y
authors.initials: Y
authors.lastname: Koide
authors.forename: N
authors.initials: N
authors.lastname: Ishida
authors.forename: M
authors.initials: M
authors.lastname: Mizugaki
mesh_terms: D000595:Amino Acid Sequence; D000903:Antibiotics, Antineoplastic / Q000032:analysis*; D001059:Apoproteins / Q000032:analysis*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D009353:Zinostatin / Q000032:analysis*
chemical_list: D000903:Antibiotics, Antineoplastic; D001059:Apoproteins; D009353:Zinostatin