Protein Identification
Protein Identification - Related Videos
08:07
Identification of Plasmodesmal Localization Sequences in Proteins In Planta
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Cited by 7 •
2017
Plant intercellular connections, the plasmodesmata (Pd), play central roles in plant physiology and plant-virus interactions. Critical to Pd transport are sorting signals that direct proteins to Pd. However, our knowledge about these sequences is still in its infancy. We describe a strategy to identify Pd localization signals in Pd-targeted proteins.
10:07
Identification of Post-translational Modifications of Plant Protein Complexes
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Cited by 8 •
2014
We describe here a protocol for the purification and characterization of plant protein complexes. We demonstrate that by immunoprecipitating a single protein within a complex, so we can identify its post-translational modifications and its interacting partners.
11:39
Identification of Functional Protein Regions Through Chimeric Protein Construction
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2019
Structurally related proteins frequently exert distinct biological functions. The exchange of equivalent regions of these proteins in order to create chimeric proteins constitutes an innovative approach to identify critical protein regions that are responsible for their functional divergence.
11:12
Identification of protein complexes with quantitative proteomics in S. cerevisiae
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Cited by 4 •
2009
Here we describe a new quantitative proteomics technique for identifying protein complexes in Saccharomyces cerevisiae. In this study, we have used the SILAC method together with affinity purification followed by tandem mass spectrometry to identify with high specificity the binding partners of an ER protein, Scs2p.
10:02
Identification of Protein Interacting Partners Using Tandem Affinity Purification
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Cited by 20 •
2012
Tandem affinity purification is a robust approach for the identification of protein binding partners. As proof of concept, this methodology was applied to the well-characterized translation initiation factor eIF4E to co-precipitate the host cell factors involved in translation initiation. This method is easily adapted to any cellular or viral protein.
FAQs
Mass spectrometry analyzes the peptide mixture produced when proteins are digested with an enzyme such as trypsin. Instead of examining only the intact protein, researchers evaluate the resulting peptide masses or sequences. This peptide-level information helps characterize which proteins contributed to a complex biological sample and supports downstream studies of cellular composition.
Gel electrophoresis separates proteins according to size or charge before further analysis. This separation can simplify a complex sample by organizing its protein components into more distinguishable groups. Researchers can then digest selected proteins into peptides and examine them by mass spectrometry, improving the organization of the identification workflow.
Antibody-based assays provide evidence through the specific binding of an antibody to its target protein. They therefore complement mass spectrometry, which analyzes peptide masses or sequences after digestion. Using these approaches together can strengthen characterization of proteins in biological samples by combining peptide-based analysis with binding-based evidence.
A typical workflow begins with a biological sample, followed by protein separation using gel electrophoresis when appropriate. Proteins are then digested into peptides with an enzyme such as trypsin, and the peptides are analyzed by mass spectrometry for their masses or sequences. Antibody-based assays may provide additional, complementary evidence.
Protein identification helps researchers examine protein expression, interactions, and modifications in cells and tissues. These dimensions connect molecular composition with cellular function rather than treating proteins as isolated entries. The resulting information can support investigation of signaling pathways and improve interpretation of complex biological samples.
In biomedical research, protein identification supports studies of disease mechanisms, biomarkers, and therapeutic targets. Examining proteins in cells and tissues can help relate molecular composition to altered biological processes. These applications make the approach relevant to both basic biology and investigations seeking molecular indicators or targets associated with disease.