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Relation between structure and function of α/β–protejns
Abstract
Protein chains are usually folded into one or several discrete globular units called domains (Schulz & Schirmer, 1979). Levitt & Chothia (1976) have shown that the structures of such domains frequently fall into one of the following three classes; α-proteins which are mainly α-helical, β-proteins which contain antiparallel β-strands and α/β proteins which have a central core consisting of a sheet of strands, most of which are parallel. The connexions between the parallel strands in αβ-proteins frequently contain helices which are packed on both sides of the sheet in a regular way (Chothia, Levitt & Richardson, 1977).
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Cited by
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,759
BIOCHEMISTRY AND GENETICS OF VON WILLEBRAND FACTOR
Sadler, J. E. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.395 · Cited by 1,363
Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
Scrutton, N. S., Berry, A., & Perham, R. N. (1990) · Nature · doi:10.1038/343038a0 · Cited by 730
Three-dimensional structure of β-galactosidase from E. coli.
Jacobson, R. H., Zhang, X.-J., DuBose, R. F., & Matthews, B. W. (1994) · Nature · doi:10.1038/369761a0 · Cited by 600
Sulfotransferases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility
Chapman, E., Best, M. D., Hanson, S. R., & Wong, C. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200300631 · Cited by 543
Metadata
- Authors
- Brändén, C.-I.
- Venue
- Quarterly Reviews of Biophysics
- Publisher
- Cambridge University Press (CUP)
- Published
- 1980-08
- Volume
- 13
- Issue
- 3
- Pages
- 317-338
- ISSN
- 0033-5835 (ISSN-L)
- 1469-8994
- OpenAlex
- W2060728728
- Cited by
- 192
- References
- 0
- FWCI
- 0.61
- Type
- journal article
- Language
- en
- Open access
- closed
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