Antibody evolution constrains conformational heterogeneity by tailoring protein dynamics
نویسندگان
چکیده
منابع مشابه
Antibody evolution constrains conformational heterogeneity by tailoring protein dynamics.
The evolution of proteins with novel function is thought to start from precursor proteins that are conformationally heterogeneous. The corresponding genes may be duplicated and then mutated to select and optimize a specific conformation. However, testing this idea has been difficult because of the challenge of quantifying protein flexibility and conformational heterogeneity as a function of evo...
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Protein-protein interactions play important roles in the control of every cellular process. How natural selection has optimized protein design to produce molecules capable of binding to many partner proteins is a fascinating problem but not well understood. Here, we performed a combinatorial analysis of protein sequence evolution and conformational dynamics to study how calmodulin (CaM), which ...
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The functions of many proteins are regulated through allostery, whereby effector binding at a distal site changes the functional activity (e.g., substrate binding affinity or catalytic efficiency) at the active site. Most allosteric studies have focused on thermodynamic properties, in particular, substrate binding affinity. Changes in substrate binding affinity by allosteric effectors have gene...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2006
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0603282103