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Protein–protein interaction and QPNC-PAGE

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between Protein–protein interaction and QPNC-PAGE

Protein–protein interaction vs. QPNC-PAGE

Protein–protein interactions (PPIs) are the physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by electrostatic forces including the hydrophobic effect. QPNC-PAGE, or quantitative preparative native continuous polyacrylamide gel electrophoresis, is a bioanalytical, high-resolution and highly accurate technique applied in biochemistry and bioinorganic chemistry to separate proteins quantitatively by isoelectric point.

Similarities between Protein–protein interaction and QPNC-PAGE

Protein–protein interaction and QPNC-PAGE have 15 things in common (in Unionpedia): Biochemistry, Conformational change, Cytochrome c, Cytoplasm, Electric field, Enzyme, Hydrogen bond, Ion, Mass spectrometry, Molecule, Monomer, Protein, Protein structure, RNA, Van der Waals force.

Biochemistry

Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms.

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Conformational change

In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors.

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Cytochrome c

The cytochrome complex, or cyt c is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion.

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Cytoplasm

In cell biology, the cytoplasm is the material within a living cell, excluding the cell nucleus.

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Electric field

An electric field is a vector field surrounding an electric charge that exerts force on other charges, attracting or repelling them.

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Enzyme

Enzymes are macromolecular biological catalysts.

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Hydrogen bond

A hydrogen bond is a partially electrostatic attraction between a hydrogen (H) which is bound to a more electronegative atom such as nitrogen (N), oxygen (O), or fluorine (F), and another adjacent atom bearing a lone pair of electrons.

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Ion

An ion is an atom or molecule that has a non-zero net electrical charge (its total number of electrons is not equal to its total number of protons).

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Mass spectrometry

Mass spectrometry (MS) is an analytical technique that ionizes chemical species and sorts the ions based on their mass-to-charge ratio.

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Molecule

A molecule is an electrically neutral group of two or more atoms held together by chemical bonds.

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Monomer

A monomer (mono-, "one" + -mer, "part") is a molecule that "can undergo polymerization thereby contributing constitutional units to the essential structure of a macromolecule".

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Protein

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.

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Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule.

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RNA

Ribonucleic acid (RNA) is a polymeric molecule essential in various biological roles in coding, decoding, regulation, and expression of genes.

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Van der Waals force

In molecular physics, the van der Waals forces, named after Dutch scientist Johannes Diderik van der Waals, are distance-dependent interactions between atoms or molecules.

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The list above answers the following questions

Protein–protein interaction and QPNC-PAGE Comparison

Protein–protein interaction has 127 relations, while QPNC-PAGE has 211. As they have in common 15, the Jaccard index is 4.44% = 15 / (127 + 211).

References

This article shows the relationship between Protein–protein interaction and QPNC-PAGE. To access each article from which the information was extracted, please visit:

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