Chemistry Faculty Publications
Document Type
Article
Abstract
Combining a single-molecule study of protein binding with a coarse grained molecular dynamics model including solvent (water molecules) effects, we find that biomolecular recognition is determined by flexibilities in addition to structures. Our single-molecule study shows that binding of CBD (a fragment of Wiskott-Aldrich syndrome protein) to Cdc42 involves bound and loosely bound states, which can be quantitatively explained in our model as a result of binding with large conformational changes. Our model identified certain key residues for binding consistent with mutational experiments. Our study reveals the role of flexibility and a new scenario of dimeric binding between the monomers: first bind and then fold. © 2007 The American Physical Society.
Repository Citation
Lu, H. Peter; Lu, Qiang; and Wang, Jin, "Exploring the Mechanism of Flexible Biomolecular Recognition with Single Molecule Dynamics" (2007). Chemistry Faculty Publications. 32.
https://scholarworks.bgsu.edu/chem_pub/32
Publication Date
2007
Publication Title
Physical Review Letters
Publisher
American Physical Society
DOI
https://doi.org/10.1103/PhysRevLett.98.128105