The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse.

Abstract excerpt

The ras binding domain (RBD) of the Ser/Thr kinase c-Raf/Raf-1 spans 78 residues and adopts a structure characteristic of the beta-grasp ubiquitin-like topology. Recently, the primary sequence of Raf RBD has been nearly exhaustively mutated experimentally by insertion of stretches of degenerate codons, which revealed sequence conservation and hydrophobic core organization similar to that found in an alignment of...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Amino Acids
• Share to Hydrophobic and Hydrophilic Interactions