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Kinases undergo conformational changes between active and inactive conformation and thus an additional hydrophobic pocket is created in the inactive conformation where the surrounding amino acids are less conserved [2].
Enzymes undergo conformational changes during the catalytic process and conformation sensitive antibodies offer a means of monitoring these changes.
Soluble Aβ initially adopts an extended conformation but at high concentrations, soluble Aβ will undergo conformational changes and form oligomers, protofibrils, and fibrils.
In the modeled structure, the finger domains from two Get3 monomers collide with each other (data not shown), suggesting that the Get3 finger domains may undergo conformational changes when the Get3 dimer switches from the open to the closed conformation.
So they undergo conformational changes.
Protein molecules often undergo conformational changes.
As suggested by our SMFS experiments (Fig. 3) during gating, these residues are expected to undergo conformational changes.
In order to perform their functions effectively and efficiently, enzymes undergo conformational changes between different functional states.
Thermal mobility and structural variations identify parts of NAT which might undergo conformational changes during catalysis.
The phosphorylated GPCR binds to an arrestin protein, and both undergo conformational changes that lead to the activation of arrestin-dependent cellular processes.
This may indicate that the 2KT/AA rings undergo conformational changes but the transitions occur gradually without bimodal height changes (Fig. 3e).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com