Gregory C. Finnigan —BIO-PROTOCOL

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Rachael Giersch Biochemistry and Molecular Biophysics, Kansas State University, USA, USA,
1 protocol

Jeremy Thorner Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, USA
1 protocol

Joëlle Schlapfer Lawrence Berkeley National Laboratory
9 protocols

Melike Çağlayan University of Florida
3 protocols

Ralph Boettcher Max Planck Institute for Biochemistry
36 protocols

Reviewer

Gregory C. Finnigan

Faculty, Kansas State University

Research focus

Molecular biology

2 Author merit
Reviewer merit
Editor merit

Lab information

https://www.k-state.edu/bmb/department/directory/finnigan/lab/

2 Protocols published

Method for Multiplexing CRISPR/Cas9 in Saccharomyces cerevisiae Using Artificial Target DNA Sequences

Authors: Rachael M. Giersch and Gregory C. Finnigan, date: 09/20/2017, view: 4621, Q&A: 0

Genome manipulation has become more accessible given the advent of the CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) editing technology. The Cas9 endonuclease binds a single stranded (single guide) RNA (sgRNA) fragment that ...

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Complex in vivo Ligation Using Homologous Recombination and High-efficiency Plasmid Rescue from Saccharomyces cerevisiae

Authors: Gregory C. Finnigan and Jeremy Thorner, date: 07/05/2015, view: 5752, Q&A: 0

The protocols presented here allow for the facile generation of a wide variety of complex multipart DNA constructs (tagged gene products, gene fusions, chimeric proteins, and other variants) using homologous recombination and in vivo ...

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2 Protocols reviewed

Trypsin Sensitivity Assay to Study the Folding Status of Proteins

Authors: Satoshi Ninagawa and Kazutoshi Mori, date: 10/05/2016, view: 4314, Q&A: 0

This protocol aims to evaluate folding status of proteins, utilizing trypsin sensitivity. Unfolded/misfolded proteins are more susceptible to trypsin than folded proteins, because trypsin easily accesses and cleaves loosely folded parts of proteins. ...

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PNGase Sensitivity Assay to Study the Folding Status of Proteins

Authors: Satoshi Ninagawa and Kazutoshi Mori, date: 10/05/2016, view: 3426, Q&A: 0

This protocol aims to evaluate folding status of proteins, utilizing peptide:N-glycanase (PNGase) sensitivity. In the cytosol, PNGase works as a deglycosylation-enzyme. N-glycans on unfolded/misfolded proteins are more susceptible to PNGase than ...

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