Periplasmic binding proteins: a versatile superfamily for protein engineering.
Publication
, Journal Article
Dwyer, MA; Hellinga, HW
Published in: Curr Opin Struct Biol
August 2004
The diversity of biological function, ligand binding, conformational changes and structural adaptability of the periplasmic binding protein superfamily have been exploited to engineer biosensors, allosteric control elements, biologically active receptors and enzymes using a combination of techniques, including computational design. Extensively redesigned periplasmic binding proteins have been re-introduced into bacteria to function in synthetic signal transduction pathways that respond to extracellular ligands and as biologically active enzymes.
Duke Scholars
Altmetric Attention Stats
Dimensions Citation Stats
Published In
Curr Opin Struct Biol
DOI
ISSN
0959-440X
Publication Date
August 2004
Volume
14
Issue
4
Start / End Page
495 / 504
Location
England
Related Subject Headings
- Structure-Activity Relationship
- Signal Transduction
- Protein Engineering
- Protein Conformation
- Periplasmic Binding Proteins
- Models, Molecular
- Ligands
- Enzymes
- Computer-Aided Design
- Biophysics
Citation
APA
Chicago
ICMJE
MLA
NLM
Dwyer, M. A., & Hellinga, H. W. (2004). Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr Opin Struct Biol, 14(4), 495–504. https://doi.org/10.1016/j.sbi.2004.07.004
Dwyer, Mary A., and Homme W. Hellinga. “Periplasmic binding proteins: a versatile superfamily for protein engineering.” Curr Opin Struct Biol 14, no. 4 (August 2004): 495–504. https://doi.org/10.1016/j.sbi.2004.07.004.
Dwyer MA, Hellinga HW. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr Opin Struct Biol. 2004 Aug;14(4):495–504.
Dwyer, Mary A., and Homme W. Hellinga. “Periplasmic binding proteins: a versatile superfamily for protein engineering.” Curr Opin Struct Biol, vol. 14, no. 4, Aug. 2004, pp. 495–504. Pubmed, doi:10.1016/j.sbi.2004.07.004.
Dwyer MA, Hellinga HW. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr Opin Struct Biol. 2004 Aug;14(4):495–504.
Published In
Curr Opin Struct Biol
DOI
ISSN
0959-440X
Publication Date
August 2004
Volume
14
Issue
4
Start / End Page
495 / 504
Location
England
Related Subject Headings
- Structure-Activity Relationship
- Signal Transduction
- Protein Engineering
- Protein Conformation
- Periplasmic Binding Proteins
- Models, Molecular
- Ligands
- Enzymes
- Computer-Aided Design
- Biophysics