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Electrostatic interactions in the GCN4 leucine zipper: substantial contributions arise from intramolecular interactions enhanced on binding.

The GCN4 leucine zipper is a peptide homodimer that has been the subject of a number of experimental and theoretical investigations into the determinants of affinity and specificity. Here, we utilize this model system to investigate electrostatic effects in protein binding using continuum calculatio...

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Bibliografiske detaljer
Main Authors: Hendsch, Z. S., Tidor, B.
Format: Artigo
Sprog:Inglês
Udgivet: Cold Spring Harbor Laboratory Press 1999
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144375/
https://ncbi.nlm.nih.gov/pubmed/10422826
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