Rationally designed helix-turn-helix proteins and their conformational changes upon DNA binding.

Circular dichroism and electrophoretic mobility shift studies were performed to confirm that dimerized N-terminal domains of bacterial repressors containing helix-turn-helix motifs are capable of high-affinity and specific DNA recognition as opposed to the monomeric N-terminal domains. Specific, hig...

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Vydáno v:	EMBO J
Hlavní autoři:	Percipalle, P, Simoncsits, A, Zakhariev, S, Guarnaccia, C, Sánchez, R, Pongor, S
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Nature Publishing Group 1995
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC394381/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7621832/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1995.tb07322.x
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