Sentence examples for basic residues at the from inspiring English sources

c-Raf seems to have a strong preference for basic residues at the −3 position and hydrophobic residues at the +1 position relative the phosphorylated serine/threonine residue.

As shown in Figure 6, the binding groove presents basic residues at the top of the cavity, acidic residues at its bottom and hydrophobic residues as edges.

In the late 80 s, Gunnar von Heijne established that membrane proteins from prokaryotes to higher eukaryotes relatively display a higher level of basic residues at the cytosol-membrane interface [23], [24], as schematized in Figure 1A.

Finally, a detailed study of the binding patches between AROS and Sirt-1 has shown that in Sirt-1 there is a conserved pharmacophore pocket composed by basic residues at the top of the cavity, acidic residues at its bottom and hydrophobic residues as edges.

The Protein kinase C (PKC), AKT kinase (Protein Kinase B), mammalian AMP-activated protein kinase, SNF1 (sucrose non-fermenting kinase 1), calcium/calmodulin-dependant kinase, phosphorylase kinase have similar preferences for basic residues at the −3 position and hydrophobic residues at the +1 position [42] [46].

The protein ligand complexes provide structural evidence for the strong preference for ligands (substrate or inhibitor) comprising basic residues at the P1 and P2 sites.

The basic residues at these positions appear to be important for interactions of the peptide with FLNa Ig21, which has a complementary acidic patch.

Alternatively, as shown for mammalian AMPK and cauliflower HMG-CoA reductase kinase [67], a basic residue at the -4 position in SnRK2 substrates may compensate for a lack of Arg at the -3 position.

An extra basic residue at the N-terminus increased retention significantly.

Using sequence-based annotation analysis, the comparison of the IML2 of UCP1 vs. that of UCP2/3 revealed that all proteins share a basic residue at the N-terminal side of the IML2.

For example, a peptide based on Ser of the Ca+2-ATPase, ACA2 [ 31], can be phosphorylated by CDPKs in vitro but lacks a basic residue at the P − 3 position (See Table 1, motif B).