Protein Design: The Choice of de Novo Sequences
Open Access
- 1 January 1997
- journal article
- review article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (4) , 2031-2034
- https://doi.org/10.1074/jbc.272.4.2031
Abstract
No abstract availableThis publication has 59 references indexed in Scilit:
- Sequence replacements in the central β‐turn of plastocyaninProtein Science, 1996
- Redesigning the Topology of a Four-Helix-Bundle Protein: Monomeric RopBiochemistry, 1995
- Core-packing constraints, hydrophobicity and protein designCurrent Opinion in Biotechnology, 1994
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Linking an Easily Detectable Phenotype to the Folding of a Common Structural MotifJournal of Molecular Biology, 1994
- The role of turns in the structure of an α-helical proteinNature, 1993
- α-Helix stability in proteinsJournal of Molecular Biology, 1992
- Systematic mutation of bacteriophage T4 lysozymeJournal of Molecular Biology, 1991
- Analysis of sequence-similar pentapeptides in unrelated protein tertiary structuresJournal of Molecular Biology, 1987
- Circular and circularly permuted forms of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1983