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Thus, artificial regulation of protein complex formation controls the cellular functions that involve protein complexes.
Many vital cellular functions are mediated by protein complex formation [1].
However, the biochemical and structural mechanism governing the Usher protein complex formation remains largely unclear.
Additional factors that might affect the efficiency of protein complex formation have been discussed previously [24].
Determining the state of protein complex formation is critical for understanding many signaling and structural pathways.
More specifically, they have been implicated as facilitators of protein complex formation [23], however, their physiological roles are largely unclear.
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Protein-protein complex formation involves removal of water from the interface region.
Furthermore, the circular dichroism spectra indicated that the fluorescence quenching mechanism might be related to arsenic-protein complex formation.
GEF-promoted nucleotide exchange involves protein-protein complex formation with large structural rearrangements.
This pointed out the importance of studying the evolution of the NP-protein complex formation and emphasized its temporal context.
An increase on ultrasonic velocity at initial stages of the reaction suggests that both conformational changes and protein-protein complex formation processes took place during the binding event.
More suggestions(15)
protein complex activities
protein body formation
protein adduct formation
protein disulfide formation
protein particle formation
protein corona formation
protein gradient formation
protein dimer formation
protein aggregate formation
protein contact formation
protein complex stoichiometry
protein complex map
protein carbonyl formation
protein complex prediction
protein network formation
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