Pub. Date : 1991 Dec
PMID : 1667734
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Derivatives of CAP having no solvent-accessible cysteine residues, or having a unique solvent-accessible cysteine residue at amino acid 2 of the helix-turn-helix motif. | Cysteine | catabolite gene activator protein | Escherichia coli |
2 | CAP contains a unique solvent-accessible cysteine residue at amino acid 10 of the helix-turn-helix motif. | Cysteine | catabolite gene activator protein | Escherichia coli |
3 | In published work, we have constructed a prototype semi-synthetic site-specific DNA cleavage agent from CAP by use of cysteine-specific chemical modification to incorporate a nucleolytic chelator-metal complex at amino acid 10 of the helix-turn-helix motif [Ebright, R., Ebright, Y., Pendergrast, P.S. | Cysteine | catabolite gene activator protein | Escherichia coli |
4 | In published work, we have constructed a prototype semi-synthetic site-specific DNA cleavage agent from CAP by use of cysteine-specific chemical modification to incorporate a nucleolytic chelator-metal complex at amino acid 10 of the helix-turn-helix motif [Ebright, R., Ebright, Y., Pendergrast, P.S. | Metals | catabolite gene activator protein | Escherichia coli |
5 | Construction of second-generation semi-synthetic site-specific DNA cleavage agents from CAP requires the construction of derivatives of CAP having unique solvent-accessible cysteine residues at sites within CAP other than amino acid 10 of the helix-turn-helix motif. | Cysteine | catabolite gene activator protein | Escherichia coli |
6 | Construction of second-generation semi-synthetic site-specific DNA cleavage agents from CAP requires the construction of derivatives of CAP having unique solvent-accessible cysteine residues at sites within CAP other than amino acid 10 of the helix-turn-helix motif. | Cysteine | catabolite gene activator protein | Escherichia coli |
7 | Construction of second-generation semi-synthetic site-specific DNA cleavage agents from CAP requires the construction of derivatives of CAP having unique solvent-accessible cysteine residues at sites within CAP other than amino acid 10 of the helix-turn-helix motif. | Cysteine | catabolite gene activator protein | Escherichia coli |
8 | In the present work, we have constructed and characterized two derivatives of CAP having no solvent-accessible cysteine residues: [Ser178]CAP and [Leu178]CAP. | Cysteine | catabolite gene activator protein | Escherichia coli |
9 | In addition, in the present work, we have constructed and characterized one derivative of CAP having a unique solvent-accessible cysteine residue at amino acid 2 of the helix-turn-helix motif: [Cys170;Ser178]CAP. | Cysteine | catabolite gene activator protein | Escherichia coli |
10 | In addition, in the present work, we have constructed and characterized one derivative of CAP having a unique solvent-accessible cysteine residue at amino acid 2 of the helix-turn-helix motif: [Cys170;Ser178]CAP. | Cysteine | catabolite gene activator protein | Escherichia coli |