Examples of using Conformational in English and their translations into Serbian
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Ecclesiastic
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Cyrillic
Binding of calcium causes a conformational change to occur in the protein.
Rotation and tilting of transmembrane α-helices may both contribute to these conformational changes.
Conformational deviations are primarily located in the four loops reaching in the ligand binding site.
The sixth residue in the loop is necessarily glycine due to the conformational requirements of the backbone.
This conformational change results in the increased affinity of the second α subunit for a second ACh ligand.
The equilibrium can favor either direction depending on ring size and other conformational effects.
The model that describes the conformational changes associated with the binding of the substrate is the alternating-access model.
The structures of BtuCD and the BtuCD homolog, HI1470/1,represent two different conformational states of an ABC transporter.
Pyrimidine dimers introduce local conformational changes in the DNA structure, which allow recognition of the lesion by repair enzymes.
During the detection of diatomic gases,the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein.
CaM undergoes a conformational change upon binding to calcium, which enables it to bind to specific proteins for a specific response.
Biochemical studies of intact transport complexes suggest that the conformational changes in the NBDs are relatively small.
These interactions induce a conformational change in the receptor structure, which triggers the activation of various intracellular signaling pathways.
The"power stroke", that is, ATP binding that induces NBD dimerization andformation of the ATP sandwich, drives the conformational changes in the TMDs.
A model that describes the conformational changes in the nucleotide-binding domain(NBD) as a result of ATP binding and hydrolysis is the ATP-switch model.
A specific nonlinear optical technique called second-harmonic generation(SHG)has been recently applied to the study of conformational change in proteins.
Reversible phosphorylation results in a conformational change in the structure in many enzymes and receptors, causing them to become activated or deactivated.
When bound, these metabolites do not participate in catalysis directly, but they are still essential:they lead to conformational changes in a concrete part of the enzyme.
Resonance is distinguished from tautomerism and conformational isomerism, which involve the formation of isomers, thus the rearrangement of the nuclear positions.
The transport cycle is initiated by binding of substrate to the high-affinity site on the TMDs,which induces conformational changes in the NBDs and enhances the binding of ATP.
Changes in quartary structure can occur through conformational changes within individual subunits or through reorientation of the subunits relative to each other.
The Q loop is presumed to be involved in the interaction of the NBD and TMD,particularly in the coupling of nucleotide hydrolysis to the conformational changes of the TMD during substrate translocation.
They are activated in response to a conformational change in the GPCR, exchanging GDP for GTP, and dissociating in order to activate other proteins in a particular signal transduction pathway.
This model proposes that the initial interaction between enzyme and substrate is relatively weak, butthat these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding.
Receptor binding induces a global conformational change that involves the movement of the two arrestin domains and the release of its C-terminal tail that contains clathrin and AP2 binding sites.
They are notable for their unusual mechanism of action,in which they irreversibly inhibit their target protease by undergoing a large conformational change to disrupt its active site.
The structures indicated that the inhibitory mechanism involved an unusual conformational change and prompted the subsequent structural focus of serpin studies.
Although a common mechanism has been suggested, the order of substrate binding,nucleotide binding and hydrolysis, and conformational changes, as well as interactions between the domains is still debated.
These proteins harness the energy of ATP binding and/or hydrolysis to drive conformational changes in the transmembrane domain(TMD) and consequently transport molecules.
Dynamins polymerize around the neck of an incoming vesicle, andtheir phosphorylation by c-SRC provides the energy necessary for the conformational change allowing the final"pinching off" from the membrane.