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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
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Spindle Assembly02:50

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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Optimizing Chromatographic Separations01:15

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Optimizing chromatographic separations is crucial for obtaining clean separations in a minimum amount of time. Optimization is required for several factors, including kinetic effects related to band broadening, plate height, capacity factor, and separation factor.
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Overview Of Cell Separation And Isolation01:20

Overview Of Cell Separation And Isolation

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Cell separation was first achieved in 1964 by S. H. Seal, who separated large tumor cells from the smaller blood cells using filtration. Two years later, Pohl and Hawk performed experiments on how cells respond differently to a nonuniform electric field based on the cell type. Such observations were the inception of cell separation methods, which allow isolating a single cell type from a heterogeneous sample.
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Native GELFrEE: a new separation technique for biomolecular assemblies.

Owen S Skinner1, Luis H F Do Vale, Adam D Catherman

  • 1Departments of Chemistry and Molecular Biosciences, the Chemistry of Life Processes Institute, the Proteomics Center of Excellence, and the Robert H. Lurie Comprehensive Cancer Center, Northwestern University , Evanston, Illinois 60208, United States.

Analytical Chemistry
|February 10, 2015
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Summary

We optimized tube gel electrophoresis and native multistage mass spectrometry (nMS/MS) for analyzing protein complexes. This method enhances the study of cellular protein organization and function.

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Area of Science:

  • Proteomics
  • Biochemistry
  • Cell Biology

Background:

  • Protein complexes are vital for cellular functions.
  • Understanding their composition and dynamics is crucial.
  • Existing separation techniques have limitations for native analysis.

Purpose of the Study:

  • To optimize tube gel electrophoresis for native multistage mass spectrometry (nMS/MS).
  • To develop a method for analyzing endogenous protein complexes from low sample amounts with high resolution.

Main Methods:

  • Tube gel electrophoresis with a cross-linking gradient and clear native buffer system.
  • Integration with native multistage mass spectrometry (nMS/MS).
  • Application to heart extracts and fungal secretomes.

Main Results:

  • Optimized tube gel separations are compatible with nMS/MS.
  • The continuous system effectively fractionates protein complexes.
  • Successful analysis of endogenous complexes from complex biological samples.

Conclusions:

  • Integrated tube gel separations and nMS/MS provide high-resolution analysis of protein complexes.
  • This approach enables untargeted proteomics at the protein complex level.
  • Advances understanding of cellular protein organization and function.