Mutations in maltose-binding protein that alter affinity and solubility properties
Mutations in maltose-binding protein that alter affinity and solubility properties
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Author / Creator
Publisher
Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag
Journal title
Language
English
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Publication information
Publisher
Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag
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Scope and Contents
Contents
Maltose-binding protein (MBP) from Escherichia coli has been shown to be a good substrate for protein engineering leading to altered binding (Marvin and Hellinga, Proc Natl Acad Sci U S A 98:4955-4960, 2001a) and increased affinity (Marvin and Hellinga, Nat Struct Biol 8:795-798, 2001b; Telmer and Shilton, J Biol Chem 278:34555-34567, 2003). It is...
Alternative Titles
Full title
Mutations in maltose-binding protein that alter affinity and solubility properties
Authors, Artists and Contributors
Author / Creator
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Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2940430
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2940430
Other Identifiers
ISSN
0175-7598
E-ISSN
1432-0614
DOI
10.1007/s00253-010-2696-y
