title: Potential use of additivity of mutational effects in simplifying protein engineering.
abstract: The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.
authors.affiliation: Structural Biology Group, Los Alamos National Laboratory, NM 87545, USA.
authors.forename: M M
authors.initials: MM
authors.lastname: Skinner
authors.forename: T C
authors.initials: TC
authors.lastname: Terwilliger
mesh_terms: D003090:Coliphages / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry*; D005583:Fourier Analysis; D008958:Models, Molecular; D017354:Point Mutation; D015202:Protein Engineering; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D004268:DNA-Binding Proteins; D014764:Viral Proteins; C069558:gene V protein, Enterobacteria phage f1