Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The primary structure of the T4 single-stranded DNA-binding protein coded by gene 32 has been determined by manual and autoated sequencing of peptides derived from partial proteolysis, cyanogen bromide cleavage, and digestion with trypsin, chymotrypsin, and staphylococcal protease. Tryptic digestion of citraconylated or succinylated gene 32 protein yields five peptides containing 4, 27, 42, 65, and 163 residues, which can be separated by Sephadex chromatography. Each of the tryptic peptides was subjected to automated sequencing and, if necessary, more extensive cleavage. The intact protein contains 301 amino acids, has a molecular weight of 33,487, and can be specifically cleaved at lysines 21 and 253 by limited trypsin digestion. Previous studies have shown that the "B" region (residues 1-21), which has a charge of +4, is important for the protein-protein interactions involved in gene 32 protein self-association and cooperaive binding to single-stranded DNA. The "A" region (residues 254-301) has been implicated in controlling the helix-destabilizing "activity" of gene 32 protein and in interacting with other T4 DNA replication proteins. The A region has a charge of -10 and, in addition, contains two unusual stretches of four serine residues separated by glycine 284. The region between positions 73 and 115 contains 75% of the tyrosine residues and may be important for DNA binding.
 ...
PMID:Amino acid sequence of the T4 DNA helix-destabilizing protein. 625 33

The amino acid sequence of the single-stranded DNA-binding protein encoded by gene 32 of bacteriophage T4 has been determined by manual and automated sequencing of peptides derived from cyanogen bromide cleavage and digestion with trypsin, chymotrypsin, and staphylococcal protease. Tryptic digestion of citraconylated or succinylated gene 32 protein yields five peptides containing 4, 27, 42, 65, and 163 residues, respectively, which can be separated by Sephadex chromatography. Each of these tryptic peptides was subjected to automated sequencing and, if necessary, more extensive cleavage. The gene 32 protein contains 301 amino acids and has a molecular weight of 33,487. Based on its primary structure, the gene 32 protein is predicted to contain 36% alpha helix, 18% beta sheet, and 46% random coil. The native protein can be specifically cleaved at lysine 21 and 253 by limited trypsin digestion. Previous studies have shown that the "B" region (residues 1 to 21) is essential for cooperative binding to single-stranded DNA. The "A" region (residues 254 to 301) has been implicated in controlling the helix-destabilizing "activity" of gene 32 protein and in interacting with other T4 DNA replication proteins. The "A" region has a net charge of -10 and, in addition, contains two unusual stretches of 4 serine residues separated by glycine 284. The region between positions 72 and 116 contains 6 of the 8 tyrosine residues in the protein and may be important for DNA binding.
 ...
PMID:Primary structure of the bacteriophage T4 DNA helix-destabilizing protein. 625 86

The amino-acid sequence of the single-stranded DNA-binding protein of bacteriophage Pf1 and the nucleotide sequence of the corresponding gene have been determined. The protein has 144 amino acids and a molecular weight of 15 400; the gene consists of 435 nucleotides. The amino-acid sequence was determined by Edman degradation, carboxypeptidase A, B, and P digestion of intact protein and of peptides derived by chymotrypsin, Staphylococcus aureus V8 protease, and trypsin digestion. The nucleotide sequence was determined by the dideoxy method after random cloning of fragments of Pf1 DNA into M13. No sequence homology could be established between the amino-acid sequence of the DNA-binding protein of Pseudomonas aeruginosa-specific bacteriophage Pf1 and bacteriophage fd of Escherichia coli.
 ...
PMID:The DNA-binding protein of Pf1 filamentous bacteriophage: amino-acid sequence and structure of the gene. 1645 14