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Chaperone (protein) and Thermolysin

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

Difference between Chaperone (protein) and Thermolysin

Chaperone (protein) vs. Thermolysin

In molecular biology, molecular chaperones are proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures. Thermolysin (Bacillus thermoproteolyticus neutral proteinase, thermoase, thermoase Y10, TLN) is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus.

Similarities between Chaperone (protein) and Thermolysin

Chaperone (protein) and Thermolysin have 2 things in common (in Unionpedia): Protein domain, Protein precursor.

Protein domain

A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain.

Chaperone (protein) and Protein domain · Protein domain and Thermolysin · See more »

Protein precursor

A protein precursor, also called a pro-protein or pro-peptide, is an inactive protein (or peptide) that can be turned into an active form by post-translational modification, such as breaking off a piece of the molecule or adding on another molecule.

Chaperone (protein) and Protein precursor · Protein precursor and Thermolysin · See more »

The list above answers the following questions

Chaperone (protein) and Thermolysin Comparison

Chaperone (protein) has 72 relations, while Thermolysin has 30. As they have in common 2, the Jaccard index is 1.96% = 2 / (72 + 30).

References

This article shows the relationship between Chaperone (protein) and Thermolysin. To access each article from which the information was extracted, please visit:

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