An analysis of integrated electromyographic (IEMG) activity of masseter and anterior temporal muscles was undertaken in fifteen patients with complete dentures and eight adult subjects with natural dentition. Bipolar surface electrodes were used for IEMG recordings during maximal voluntary clenching and saliva swallowing in the inter-cuspal position. The IEMG activity of both muscles during maximal voluntary clenching was significantly lower in patients with complete dentures than in subjects with natural dentition. During saliva swallowing the activity in both muscles was similar in both groups. This may have a great clinical significance in the maintenance of the functional state of the different structures of the stomatognathic system in complete denture wearers, since the process of swallowing is a 24-h function repeated about 600-2400 times each day.

An analysis of integrated electromyographic (IEMG) activity of the superior orbicularis oris muscle was undertaken in 15 children with cleft lip and palate who have undergone surgery compared to 10 children without clefts (control group). Bipolar surface electrodes were used for IEMG recordings of resting level activity and during the swallowing of saliva. Similar resting level activity was observed in both groups. During the swallowing of saliva, activity in children with cleft lip and palate was higher than in children without clefts (noncleft children). Moreover, in the cleft lip and palate group, children with abnormal lip seal showed the highest values for IEMG activity during the swallowing of saliva. This fact suggests that with each swallow of saliva, a greater counteracting effect of the superior orbicularis oris muscle could be produced on the growing maxilla. This may result in a significant long-term effect on the growth of the stomatognathic system, since the process of swallowing is a 24-hour function repeated between 600 and 2400 times each day.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the key CO2-fixing enzyme in photosynthesis, is notorious for its low carboxylation. We report a highly active and assembly-competent Form II Rubisco from the endosymbiont of a deep-sea tubeworm Riftia pachyptila (RPE Rubisco), which shows a 50.5% higher carboxylation efficiency than that of a high functioning Rubisco from Synechococcus sp. PCC7002 (7002 Rubisco). It is a simpler hexamer with three pairs of large subunit homodimers around a central threefold symmetry axis. Compared with 7002 Rubisco, it showed a 3.6-fold higher carbon capture efficiency in vivo using a designed CO2 capture model. The simple structure, high carboxylation efficiency, easy heterologous soluble expression/assembly make RPE Rubisco a ready-to-deploy enzyme for CO2 capture that does not require complex co-expression of chaperones. The chemosynthetic CO2 fixation machinery of chemolithoautotrophs, CO2-fixing endosymbionts, may be more efficient than previously realized with great potential for next-generation microbial CO2 sequestration platforms.

Cephalometric measurements and electromyographic analysis of the superior orbicularis oris muscle were undertaken in 13 children with unilateral cleft lip and palate with a short upper lip length who have undergone surgery in childhood. Initially, cephalometric and electromyographic records were evaluated and again after the subjects had continuously worn, for 4 months, a removable appliance specially designed to avoid the restraining effect of superior orbicularis oris muscle activity over the maxilla. Comparison between pretreatment and posttreatment cephalometric measurements showed a significant improvement in both the sagittal position of the maxilla and the dentoalveolar position. No significant changes were observed in electromyographic activity during rest or when saliva swallowing. Cephalometric changes suggest that the removable appliance used improves the growth of the maxilla.

Cold shock proteins (Csp) constitute a family of ubiquitous small proteins that act as RNA-chaperones to avoid cold-induced termination of translation. All members contain two subdomains composed of 2 and 3 β-strands respectively, which are connected by a hinge loop and fold into a β-barrel. Bacillus caldolyticus Csp (BcCsp) is one of the most studied members of the family in terms of its folding, function and structure. This protein has been described as a monomer in solution, although a recent crystal structure showed dimerization via domain swapping (DS). In contrast, other cold shock proteins of the same fold are known to dimerize in a non-swapped arrangement. Hypothesizing that reducing the size of the hinge loop may promote swapping as in several other DS proteins with different folds we deleted two residues from these region (BcCspΔ36–37), leading to a protein in monomer-dimer equilibrium with similar folding stability to that of the wild-type. Strikingly, the crystal structure of BcCspΔ36–37 revealed a non-swapped dimer with its interface located at the nucleic acid-binding surface, showing that the deletion led to structural consequences far from the perturbation site. Concomitantly, circular dichroism experiments on BcCspΔ36–37 demonstrated that binding of the oligonucleotide hexathymidine disrupts the dimer. Additionally, HDXMS shows a protective effect on the protein structure upon dimerization, where the resulting interactions between ligand-binding surfaces in the dimer reduced the extent of exchange throughout the whole protein. Our work provides evidence of the complex interplay between conformational dynamics, deletions and oligomerization within the Csp protein family.