Literature DB >> 12559589

Oriented versus random protein immobilization.

Meir Wilchek1, Talia Miron.   

Abstract

Immobilization of proteins on solid surfaces plays an important role in all the fields of modern biology. Two approaches are used in the immobilization of proteins: a random and an oriented mode of binding to solid matrices. In this note, we show that there is not much difference in using either mode of immobilization, since proteins usually bind to a matrix through only one or two bonds. This is demonstrated by the attachment of several proteins to CNBr-activated Sepharose through their lysines and the consequent conversion of those lysines to homoarginine upon treatment with ammonium hydroxide.

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Year:  2003        PMID: 12559589     DOI: 10.1016/s0165-022x(02)00178-1

Source DB:  PubMed          Journal:  J Biochem Biophys Methods        ISSN: 0165-022X


  7 in total

1.  Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments.

Authors:  Lei Gu; Sam Ngo; Zhefeng Guo
Journal:  J Biol Chem       Date:  2012-01-25       Impact factor: 5.157

2.  Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins.

Authors:  Carlos J López; Mark R Fleissner; Zhefeng Guo; Ana K Kusnetzow; Wayne L Hubbell
Journal:  Protein Sci       Date:  2009-08       Impact factor: 6.725

3.  Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry.

Authors:  Chunling Wa; Ron L Cerny; David S Hage
Journal:  Anal Chem       Date:  2006-12-01       Impact factor: 6.986

4.  Sortase-mediated immobilization of Candida antarctica lipase B (CalB) on graphene oxide; comparison with chemical approach.

Authors:  Faezeh Moosavi; Faezeh Ahrari; Gholamreza Ahmadian; Mehdi Mohammadi
Journal:  Biotechnol Rep (Amst)       Date:  2022-04-21

5.  Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.

Authors:  Carlos J López; Mark R Fleissner; Evan K Brooks; Wayne L Hubbell
Journal:  Biochemistry       Date:  2014-11-05       Impact factor: 3.162

6.  Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study.

Authors:  Sam Ngo; Vicky Chiang; Elaine Ho; Linh Le; Zhefeng Guo
Journal:  PLoS One       Date:  2012-10-16       Impact factor: 3.240

7.  Arginine-to-lysine substitutions influence recombinant horseradish peroxidase stability and immobilisation effectiveness.

Authors:  Barry J Ryan; Ciarán O'Fágáin
Journal:  BMC Biotechnol       Date:  2007-12-05       Impact factor: 2.563

  7 in total

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