Skip to main content
Advertisement
Browse Subject Areas
?

Click through the PLOS taxonomy to find articles in your field.

For more information about PLOS Subject Areas, click here.

< Back to Article

Local Conformational Changes in the DNA Interfaces of Proteins

Figure 5

Propensities of the amino acid residues.

(a) Conformationally changed fragments vs. conformationally unchanged fragments in DNA interfaces (filled bar) and non-interfaces (open). A positive value indicates that frequency that amino acid is observed in conformationally changed fragments is higher than that in conformationally unchanged fragments. (b) DNA interfaces vs. non-interfaces for conformationally changed fragments (filled) and conformationally unchanged fragments (open). A positive value indicates that frequency that amino acid is observed in DNA interfaces is higher than that in non-interfaces. Error bar indicates the 85% bootstrap confidence interval. The background colors denote the physico-chemical property of amino acids: hydrophobic is shown in pale green; polar in pink; basic in blue; acidic in red.

Figure 5

doi: https://doi.org/10.1371/journal.pone.0056080.g005