Characterization of secondary structure of neocarzinostatin apoprotein.
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.
Saito
K
K
Sato
Y
Y
Edo
K
K
Akiyama-Murai
Y
Y
Koide
Y
Y
Ishida
N
N
Mizugaki
M
M
D000595:Amino Acid Sequence; D000903:Antibiotics, Antineoplastic / Q000032:analysis*; D001059:Apoproteins / Q000032:analysis*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D009353:Zinostatin / Q000032:analysis*
D000903:Antibiotics, Antineoplastic; D001059:Apoproteins; D009353:Zinostatin