Words similar to phe
Example sentences for: phe
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This binding site coincides with that of AChBP, and is in agreement with photo-affinity labeling and mutagenesis study [ 6 11 ] . The ligand makes Van der Waals contact with Trp182, Tyr230 and Cys225-226 of alpha4, and Trp82, Leu146 and Phe144 of beta2 (Figure 3- Top).
The p51 subunit is generated via endoproteolytic cleavage of the p66 subunit between Phe 440 and Tyr 441 [ 5 6 ] . The larger subunit (p66) contains both polymerase and RNase H activities, while the smaller subunit (p51) lacks these functions, in context of the heterodimer [ 7 8 ] . However, both the p66 and p51 monomers are functionally inactive when dissociated from each other [ 9 ] . Several years have passed since it was first suggested that agents that could specifically disrupt the dimerization of HIV-1 RT might prove a worthwhile antiretroviral strategy [ 10 ] , though such agents have yet to be developed.
1B, the interface of the dimers consists of an apolar core comprised of Met57, Ala61, Leu64, and Leu65 on the ML surface and Phe45, Leu47, Val80 and Leu84 on the EH surface.
For 10 of the 18 amino acids with more than one codon (Arg, Asn, His, Ile, Leu, Lys, Phe, Pro, Thr, Tyr), the most frequently used codon in D. willistoni differs from that in D. melanogaster . All 10 of these changes in synonymous codon usage involve D. willistoni most frequently using an A- or T-ending (or beginning, for example, Leu) codon with D. melanogaster using a G- or C-ending (or beginning) codon, supporting a trend identified originally using only the Adh coding sequence [ 41].
All crystallographically characterized metallo-β-lactamases have a flexible amino acid chain that extends over the active site [ 37 42 44 45 46 47 48 49 ] . Previous NMR studies on CcrA have shown that this loop "clamps down" on substrate or inhibitor upon binding, and there is speculation that the distortion of substrate upon clamping down of the loop may drive catalysis [ 50 ] . The crystal structure of L1 showed that there is a large loop that extends over the active site, and modeling studies have predicted that two residues, Ile164 and Phe158, make significant contacts with large, hydrophobic substituents at the 2' or 6' positions on penicillins, cephalosporins, or carbapenems [ 37 ] . To test this prediction, Ile 164 and Phe158 were changed from large, hydrophobic residues to alanines to afford the I164A and F158A mutants.
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