Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2828644 | Journal of Structural Biology | 2012 | 11 Pages |
Abstract
Homology models were built for various length sequences of the kinesin-1 light chain (KLC) domain of Drosophila melanogaster and subjected to 200 ns of all-atom molecular dynamics. We also cloned, expressed and characterized these regions spectroscopically. Results confirm that KLC contains tetratricopeptide repeat units; a regular array of repeating 34-residue helix–loop–helix monomers. Experimental and computational evidence is provided confirming the stability and overall helicity of individual TPR repeats as well as individual TPR units incorporated into a multi-TPR structure.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
Sally Q. Fisher, Meredith Weck, Jenna E. Landers, Jeffrey Emrich, Shana A. Middleton, Jordan Cox, Lisa Gentile, Carol A. Parish,