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A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.

The leucine zipper is a dimeric coiled-coil protein structure composed of two amphipathic alpha-helices with the hydrophobic surfaces interacting to create the dimer interface. This structure has been found to mediate the dimerization of two abundant classes of DNA binding proteins: the bZIP and bHL...

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Hlavní autoři: Krylov, D, Mikhailenko, I, Vinson, C
Médium: Artigo
Jazyk:Inglês
Vydáno: 1994
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC395166/
https://ncbi.nlm.nih.gov/pubmed/8026470
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