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pro vyhledávání: '"Gautham Varadamsetty"'
Autor:
Gautham Varadamsetty, Christina Ewald, Pietro Alfarano, Amedeo Caflisch, Riccardo Pellarin, Oliver Zerbe, Fabio Parmeggiani, Andreas Plückthun
Publikováno v:
Protein Science. 21:1298-1314
A multidisciplinary approach based on molecular dynamics (MD) simulations using homology models, NMR spectroscopy, and a variety of biophysical techniques was used to efficiently improve the thermodynamic stability of armadillo repeat proteins (ArmRP
Autor:
Gautham Varadamsetty, Andreas Plückthun, Peer R. E. Mittl, Markus G. Grütter, Chaithanya Madhurantakam
Publikováno v:
Protein Science. 21:1015-1028
The armadillo domain is a right-handed super-helix of repeating units composed of three α-helices each. Armadillo repeat proteins (ArmRPs) are frequently involved in protein–protein interactions, and because of their modular recognition of extende
Autor:
Fabio Parmeggiani, Anders Peter Larsen, Riccardo Pellarin, Michael T. Stumpp, Gautham Varadamsetty, Andreas Plückthun
Publikováno v:
Journal of Molecular Biology
Designed Armadillo repeat proteins (ArmRPs) are a novel class of binding proteins intended for general modular peptide binding and have very favorable expression and stability properties. Using a combination of sequence and structural consensus analy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3179f40cb87714a52dca871901bfa5b7
https://www.zora.uzh.ch/id/eprint/68464/
https://www.zora.uzh.ch/id/eprint/68464/
Autor:
Oliver Zerbe, Riccardo Pellarin, Gautham Varadamsetty, Andreas Plückthun, Anders Peter Larsen, Michael T. Stumpp, Amedeo Caflisch, Fabio Parmeggiani
Armadillo repeat proteins are abundant eukaryotic proteins involved in several cellular processes, including signaling, transport, and cytoskeletal regulation. They are characterized by an armadillo domain, composed of tandem armadillo repeats of app
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26897af729a03141f04f677500ac0954
Publikováno v:
Journal of Molecular Biology. 425:969-970