Sentence examples for open cleft from inspiring English sources
The open cleft of 1 selectively recognizes tetrabutylammonium dihydrogen phosphate in CH3CN by exhibiting a significant decrease in the emission of anthracene.
CBHs bind the cellulose chain in a more or less closed tunnel and cleave off cellobiose units processively from one end of the cellulosic polymer, while endoglucanases have their active sites in a more or less open cleft and show a higher tendency to cut bonds internally in the polymer.
A-states, which have weak actin affinity, have an open cleft while R-states, which bind strongly to actin, have a closed cleft [1].
In Ref.[21], a model of CelS in the product state was constructed by filling the open cleft (subsites +1, +2) of the CelS-cellohexaose complex with cellobiose from the CelS-product complex and these coordinates were used for the product state in the present work.
The single-peptide binding mode follows a canonical ligand binding mechanism, i.e., binding to an open cleft between the EF and BG loops.
Type B CBMs have an open cleft that can bind polysaccharides found in amorphous regions of cellulose and hemicellulose [ 43– 43].
The directed hydrogen bonds (both conventional and unconventional) and charge charge interactions allowed the open clefts of both 1 and 2 to bind carboxylate, fluoride and dihydrogenphosphate anions with moderate binding constant values.
The substrate-binding site in chondroitinase ABC I is in a wide-open cleft, consistent with the endolytic action pattern of this enzyme.
The opened cleft has been proposed as the binding site for a hypothetical facilitator of prion conversion that may play a role in pathogenic PrPSc formation [23], [24].
On ATP hydrolysis, domain 1A would be the one releasing its DNA and rebinding it at the +1 nt register, restoring the initial open-cleft conformation.
In the case of AFEX-CS and IL-CS, both exocellulases (CBH I and CBH II) had higher recovery after 48 h compared to EG I. We speculate that the increased non-productive interaction of endocellulases like EG I towards lignin could be due to the more open-cleft active site accessibility of aromatic amino acid residues that facilitates hydrophobic interaction with lignin [ 24].
