Characterization of secondary structure of neocarzinostatin apoprotein
| Autor: | Yuriko Akiyama-Murai, Kunihito Saito, Yukio Sato, Nakao Ishida, Kiyoto Edo, Yoshio Koide, Michinao Mizugaki |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Conformational change Antibiotics Antineoplastic Neocarzinostatin Protein Conformation Stereochemistry Molecular Sequence Data Peptide General Chemistry General Medicine behavioral disciplines and activities chemistry.chemical_compound Protein structure Zinostatin chemistry mental disorders Drug Discovery medicine Amino Acid Sequence Sodium dodecyl sulfate Apoproteins Protein secondary structure Peptide sequence medicine.drug |
| Zdroj: | Chemical and Pharmaceutical Bulletin. 37:3078-3082 |
| ISSN: | 1347-5223 0009-2363 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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