Literature DB >> 25859952

Detecting protein-protein interactions by gel filtration chromatography.

Yan Bai1.   

Abstract

Upon protein-protein interaction, the formed complex is subject to a change in size. A number of methods can be utilized to detect such a change. Gel filtration technology is well recognized for its ability to monitor and separate protein species of different sizes, and can greatly facilitate functional studies of protein complexes. In addition, gel filtration can be performed in any buffer system that preserves the protein complex formation and function. Therefore, it can be a significantly useful method for studying protein interactions. In this chapter, a protocol for performing gel filtration is described in detail.

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Year:  2015        PMID: 25859952     DOI: 10.1007/978-1-4939-2425-7_13

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  3 in total

Review 1.  An Overview of Current Methods to Confirm Protein-Protein Interactions.

Authors:  Kenji Miura
Journal:  Protein Pept Lett       Date:  2018       Impact factor: 1.890

Review 2.  Molecular basis for protein-protein interactions.

Authors:  Brandon Charles Seychell; Tobias Beck
Journal:  Beilstein J Org Chem       Date:  2021-01-04       Impact factor: 2.883

3.  Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis.

Authors:  Chandana Peddu; Sufang Zhang; Hong Zhao; Agnes Wong; Ernest Y C Lee; Marietta Y W T Lee; Zhongtao Zhang
Journal:  iScience       Date:  2018-07-18
  3 in total

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