Sentence examples for cc structure from inspiring English sources

Cytoskeletal intermediate filaments (IFs) assemble from the elementary dimers based on a segmented α-helical coiled-coil (CC) structure.

Subsequently, the filtration process and the wicking ability of paper enabled to freeze the deposited CC structure inherited from the suspension.

Compared with the water-only cyclones with single cone structure, the separation performance of the CCS with CC structure was significantly improved and much less losses of + 0.25 mm low density coarse coal were resulted.

The first CC structure was solved by cryo-electron microscopy (cryo-EM) at 15 Å resolution (Fronzes et al, 2009).

Furthermore, our observations have obvious relevance to human skeletal diseases such as cleidocranial dysplasia in which the polyQ/polyA CC structure of RUNX2 is extended by polyA expansion.

The CC subdomain, however, displays a relatively large deviation (0.9 Å), which is associated with bending of a long CC structure and resulted in large average r.m.s.

As predictable for CC structures, the CC helical folding was considerably stabilized by the addition of canonical hydrophobic residues in position a/d of the polyA stretch (peptide ccAL, Fig.  2B and C) and completely disrupted by prolines at the same positions (peptide ccAP), as shown by a single minimum at ∼200 nm indicating a random coil conformation (Fig.  2B).

Our experiments show that, besides being significantly associated in eukaryotic proteomes, polyQ and polyA repeat share a common structural propensity to form α-helical CC structures.

In the potential region between 0 and −0.9 V vs. Ag/AgCl/KCl (3 M) a broad band assigned to CC structures is observed in the triple-bond region (∼1900 cm−1, FWHM = 180 cm−180

Other retroviral IN CC structures display the same dimer boundary, indicating that this type of interface is biologically relevant.

Besides polymerization and aggregation, CC structures can mediate also homotypic and heterotypic protein protein interactions (16).