Biochemical Journal · 1984 · 82 citations · 12 references
BiochemistryStructural BioinformaticsProtein FoldingMany Cysteine ProteinasesSecondary StructureNatural SciencesMedicineMolecular BiologyBiomolecular Structure PredictionProtein Structure PredictionAmino Acid SequenceProteomicsStructural Biology
The amino acid sequence of cystatin, the protein from chicken egg-white that is a tight-binding inhibitor of many cysteine proteinases, is reported. Cystatin is composed of 116 amino acid residues, and the Mr is calculated to be 13 143. No striking similarity to any other known sequence has been detected. The results of computer analysis of the sequence and c.d. spectrometry indicate that the secondary structure includes relatively little alpha-helix (about 20%) and that the remainder is mainly beta-structure.
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Atlas of Protein Sequence and Structure, 1972.
Walter M. Fitch, M. O. Dayhoff · Systematic Zoology · 1973 · 2.5K citations
Peter Y. Chou, Gerald D. Fasman · Biophysical Journal · 1979 · 355 citations · Full text