Pub. Date : 2007 Oct
PMID : 17897208
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Identification of amino acids involved in the Flo11p-mediated adhesion of Saccharomyces cerevisiae to a polystyrene surface using phage display with competitive elution. | Polystyrenes | Flo11p | Saccharomyces cerevisiae S288C |
| 2 | AIMS: To identify the main amino acids involved in the Flo11p-mediated adhesion of Saccharomyces cerevisiae to the polystyrene surface PolySorp. | Polystyrenes | Flo11p | Saccharomyces cerevisiae S288C |
| 3 | Tryptophan and proline were more abundant in the peptides of phages from competitive elution with FLO11 cells than in those from competitive elution with flo11Delta cells. | Tryptophan | Flo11p | Saccharomyces cerevisiae S288C |
| 4 | Tryptophan and proline were more abundant in the peptides of phages from competitive elution with FLO11 cells than in those from competitive elution with flo11Delta cells. | Proline | Flo11p | Saccharomyces cerevisiae S288C |
| 5 | Furthermore, two phages with hydrophobic peptides containing 1 or 2 tryptophan, and 3 or 5 proline, residues inhibited the adhesion of FLO11 cells to PolySorp more than a phage with a hydrophobic peptide containing no tryptophan and only two proline residues. | Tryptophan | Flo11p | Saccharomyces cerevisiae S288C |
| 6 | Furthermore, two phages with hydrophobic peptides containing 1 or 2 tryptophan, and 3 or 5 proline, residues inhibited the adhesion of FLO11 cells to PolySorp more than a phage with a hydrophobic peptide containing no tryptophan and only two proline residues. | Proline | Flo11p | Saccharomyces cerevisiae S288C |
| 7 | Furthermore, two phages with hydrophobic peptides containing 1 or 2 tryptophan, and 3 or 5 proline, residues inhibited the adhesion of FLO11 cells to PolySorp more than a phage with a hydrophobic peptide containing no tryptophan and only two proline residues. | Tryptophan | Flo11p | Saccharomyces cerevisiae S288C |
| 8 | Furthermore, two phages with hydrophobic peptides containing 1 or 2 tryptophan, and 3 or 5 proline, residues inhibited the adhesion of FLO11 cells to PolySorp more than a phage with a hydrophobic peptide containing no tryptophan and only two proline residues. | Proline | Flo11p | Saccharomyces cerevisiae S288C |
| 9 | CONCLUSIONS: Our results suggest a key role of tryptophan and proline in the hydrophobic interactions between Flo11p on the S. cerevisiae cell surface and the PolySorp surface. | Tryptophan | Flo11p | Saccharomyces cerevisiae S288C |
| 10 | CONCLUSIONS: Our results suggest a key role of tryptophan and proline in the hydrophobic interactions between Flo11p on the S. cerevisiae cell surface and the PolySorp surface. | Proline | Flo11p | Saccharomyces cerevisiae S288C |