title: Computational design of intermolecular stability and specificity in protein self-assembly.
abstract: The ability to engineer novel proteins using the principles of molecular structure and energetics is a stringent test of our basic understanding of how proteins fold and maintain structure. The design of protein self-assembly has the potential to impact many fields of biology from molecular recognition to cell signaling to biomaterials. Most progress in computational design of protein self-assembly has focused on α-helical systems, exploring ways to concurrently optimize the stability and specificity of a target state. Applying these methods to collagen self-assembly is very challenging, due to fundamental differences in folding and structure of α- versus triple-helices. Here, we explore various computational methods for designing stable and specific oligomeric systems, with a focus on α-helix and collagen self-assembly.
authors.affiliation: Department of Biochemistry, Robert Wood Johnson Medical School, UMDNJ, Piscataway, New Jersey, USA.
authors.forename: Vikas
authors.initials: V
authors.lastname: Nanda
authors.forename: Sohail
authors.initials: S
authors.lastname: Zahid
authors.forename: Fei
authors.initials: F
authors.lastname: Xu
authors.forename: Daniel
authors.initials: D
authors.lastname: Levine
mesh_terms: D019295:Computational Biology; D003198:Computer Simulation; D006801:Humans; D008958:Models, Molecular; D017510:Protein Folding; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D011506:Proteins