Volume 22, Issue 10
October 2009
Cover image
Cover image
cover illustration Affinity of the displayed peptide in landscape phage can be modulated by mutations in the major coat protein.A short length of the phage surface according to the model of Marvin et al. (1994) composed of major coat protein subunits. White areas show guest peptides, grey and red - intact phage amino acids, yellow - mutagenized segment exposed at the phage surface. For further details see Kuzmicheva et al., page 631-639.
ISSN 1741-0126
EISSN 1741-0134
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Volume 22, Issue 10, October 2009
Original articles
Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 587–596, https://doi.org/10.1093/protein/gzp024
Evaluation of folding co-operativity of a chimeric protein based on the molecular recognition between polyproline ligands and SH3 domains
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 597–606, https://doi.org/10.1093/protein/gzp041
Tying up the loose ends: circular permutation decreases the proteolytic susceptibility of recombinant proteins
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 607–613, https://doi.org/10.1093/protein/gzp034
Enzyme stabilization by domain insertion into a thermophilic protein
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 615–623, https://doi.org/10.1093/protein/gzp044
Tubulin isotype specificity and identification of the epitope for antibody Tub 2.1
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 625–629, https://doi.org/10.1093/protein/gzp046
Mutations in fd phage major coat protein modulate affinity of the displayed peptide
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 631–639, https://doi.org/10.1093/protein/gzp043
Design, expression and characterization of mutants of fasciculin optimized for interaction with its target, acetylcholinesterase
Protein Engineering, Design and Selection, Volume 22, Issue 10, October 2009, Pages 641–648, https://doi.org/10.1093/protein/gzp045
