Related Experiment Video
Updated: Jun 15, 2026

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
Published on: July 6, 2014
Why inverse proteins are relatively abundant
Jean-Christophe Nebel1, Claude Godfrey Charles Walawage
1Faculty of Computing, Information Systems and Mathematics, Kingston University, Kingston-upon-Thames, KT1 2EE, UK. J.Nebel@kingston.ac.uk
Abstract:
Studies have shown that inverse proteins are relatively abundant. In this work, we investigate the proposition that the repeat patterns they share with protein sequences explain this phenomenon. Using a new artificial set of peptide sequences which also display these features and a random set, we show that the presence of repeats contributes to protein sequence similarity. Further analysis confirms that most inverse proteins exhibit repeats. Therefore, we suggest the relative abundance of inverse proteins can be explained by the fact they display the same repeat structures and amino acid propensity of existing proteins.
Related Concept Videos
Globular Proteins
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Intrinsically Disordered Proteins
Intrinsically Disordered Proteins
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Drug Distribution: Plasma Protein Binding

