Sentence examples for movement of loop from inspiring English sources

Dimeric form of PfCS was generated and the FMN binding mechanism involving movement of loop near active site has been proposed.

The coordinates derived by electron crystallographic analysis of the late intermediate analog 1FBK show the largest movement of loop EF (marked "3" in Fig. 3).

Further, in hMtb-BirA (as well as 2cgh), the side chains of the residue E123 and neighboring residues R135 & R215 are not defined beyond Cβ but they are well defined in the subunit A of dhMtb-BirA, a consequence probably of outward movement of loop L6.

Additionally, substrate binding may be prevented by conformational changes that occlude the substrate binding pocket, such as movement of loop residues 14 27 in KSHV Pr.

The increased size of this gap is also due to the movement of loop Pro Ala away from the entrance on the opposite side of the C-terminal helix, so that the protein backbone and Gln are not restrictive.

Similarly, 'spacer' residues may be important to allow movement of loop C, as a bulky hydrophobic side chain was preferred at position 187 (loop B), and our homology models suggest van der Waals contacts between the side chain of Ile-187 and residues within the β9 and β10 strands (loop C) of the same subunit.

The alternating and repetitive movement of loops at specific times is consistent with the presence of 11 defined hydrogen bonds.

These motions in turn drive axial movement of loops lining the hexamer pore (pore loops), which contain aromatic residues that directly engage substrate proteins during unfolding (Siddiqui et al., 2004; Iosefson et al., 2015).

In addition, movements of loop 1 produced when the tRNAi enters the PIN state would disrupt some interactions between this loop and rRNA shown previously to be important for tight binding of eIF1 to the 40S subunit (Martin-Marcos et al., 2013).

Upon this movement, the grooves harbouring conserved MotB residues (including Asp164 and Leu179 implicated in binding to the peptide moiety of PG) open up making them accessible to PG. Motion profile 2 (Chain E mode 2, Fig. 3(B)) accounts for 13% of the overall motion and is dominated by the movements of loops β2α2 and β3β4 resulting in the opening of the cleft between these two loops.

The movements of loops and secondary structure elements can provide an energetically favorable method of controlling access for larger ligands.