Title : Folding and misfolding of the papillomavirus E6 interacting peptide E6ap.

Pub. Date : 2003 Jun 10

PMID : 12771374






1 Functional Relationships(s)
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1 Six independent folding trajectories, with a total duration of nearly 2 micros, all lead to the same native state in which the E6ap adopts a fluctuating alpha-helix structure in the central portion (Ser-4-Leu-13) but with very flexible N and C termini. Serine ubiquitin protein ligase E3A Homo sapiens