title: Weakly stable regions and protein-protein interactions in beta-barrel membrane proteins.
abstract: We briefly discuss recent progress in computational characterization of the sequence and structural properties of β-barrel membrane properties. We discuss the emerging concept of weakly stable regions in β-barrel membrane proteins, computational methods to identify these regions and mechanisms adopted by β-barrel membrane proteins in nature to stabilize them. We further discuss computational methods to identify protein-protein interactions in β-barrel membrane proteins and recent experimental studies that aim at altering the biophysical properties including oligomerization state and stability of β-barrel membrane proteins based on the emerging organization principles of these proteins from recent computational studies.
authors.forename: Hammad
authors.initials: H
authors.lastname: Naveed
authors.affiliation: Department of Bioengineering, University of Illinois at Chicago, Chicago, IL, 60607, USA. jliang@uic.edu.
authors.forename: Jie
authors.initials: J
authors.lastname: Liang
mesh_terms: D001665:Binding Sites; D001703:Biophysics; D019295:Computational Biology; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D025941:Protein Interaction Mapping / Q000379:methods*; D055503:Protein Multimerization; D055550:Protein Stability
chemical_list: D008565:Membrane Proteins