Potential Use of Additivity of Mutational Effects in Simplifying Protein Engineering

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 addit...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1996-10, Vol.93 (20), p.10753-10757
Main Authors: Skinner, Matthew M., Terwilliger, Thomas C.
Format: Article
Language:English
Subjects:
Additive effects
Amino acid substitution
Amino acids
Atoms
Biochemistry
Coliphages - chemistry
Coordinate systems
DNA-Binding Proteins - chemistry
Electron density
Fourier Analysis
Genetic mutation
Models, Molecular
Molecules
phage f1
Point Mutation
Protein Engineering
Protein Structure, Tertiary
Structure-Activity Relationship
Viral Proteins - chemistry
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.93.20.10753