Sentence examples for helix facing from inspiring English sources

Inspection of the crystal structures of several kinases revealed that the closest residue in space to the homologous V617 position frequently resided in the middle of the αC helix, on the face of the helix facing the homologous V617 residue (Figure 1A and B).

An anti-parallel pair is defined as the N-term of each helix facing a different localization, otherwise it is a parallel pair.

While this similarity in the S4 S5 linker is remarkable on its own, it also promotes our confidence in an S6 helix facing T635 despite a low overall sequence identity.

TT dinucleotides are observed approximately 5 bp in either direction of the AA dinucleotides, as this is the position where the complementary helix faces the core complex.

Two recently published, independent studies, one by Segal et al. [ 1] and one by Ioshikhes et al. [ 2], present evidence that the primary DNA sequence can facilitate the bending of the helix around the histone octamer by presenting AA dinucleotides at those positions where the phosphodiester backbone of the helix faces towards the histone core.

These findings suggested that parallel coiled-coils will most like be formed and, hence, each of the negatively charged residues of one alpha-helix faces the positively charged residues of the neighboring alpha-helix, and vice versa (Figure 5B).

To this goal, the analogues were designed to increase only net positively charge by Lys-substitution of positions 2, 9, 13, or 16 at the hydrophilic helix face of CRAMP-18 without any change at the hydrophobic helix face.

A l- or d-Pro substitution (KLW-L9P or KLW-L9p) of Leu9 at the hydrophobic helix face of KLW induced a more significant reduction in hemolytic activity with improved antibacterial activity than that (KLW-K11P or KLW-K11p) of Lys11 in the hydrophilic helix face.

To investigate the effects of l- or d-Pro kink incorporation into hydrophobic or hydrophilic helix face of KLW on structure, cell selectivity, and membrane-binding affinity, we designed a series of four peptides, in which Leu9 and Lys11 in the hydrophobic and hydrophilic helix face of KLW, respectively, are substituted with l- or d-Pro.

Our results collectively suggest that d-Pro incorporation into the hydrophobic helix face of non-cell selective amphipathic α-helical peptides may be useful for the design of novel antimicrobial peptides possessing high bacterial cell selectivity without hemolytic activity.

Together, this analysis suggests that Lsm1-7-Pat1C conlyex may only bind RNA from the helix face.