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Lysine and Salt bridge (protein and supramolecular)

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

Difference between Lysine and Salt bridge (protein and supramolecular)

Lysine vs. Salt bridge (protein and supramolecular)

Lysine (symbol Lys or K) is an α-amino acid that is used in the biosynthesis of proteins. In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1).

Similarities between Lysine and Salt bridge (protein and supramolecular)

Lysine and Salt bridge (protein and supramolecular) have 4 things in common (in Unionpedia): Aspartic acid, Chirality (chemistry), Glutamic acid, Hydrogen bond.

Aspartic acid

Aspartic acid (symbol Asp or D; salts known as aspartates), is an α-amino acid that is used in the biosynthesis of proteins.

Aspartic acid and Lysine · Aspartic acid and Salt bridge (protein and supramolecular) · See more »

Chirality (chemistry)

Chirality is a geometric property of some molecules and ions.

Chirality (chemistry) and Lysine · Chirality (chemistry) and Salt bridge (protein and supramolecular) · See more »

Glutamic acid

Glutamic acid (symbol Glu or E) is an α-amino acid with formula.

Glutamic acid and Lysine · Glutamic acid and Salt bridge (protein and supramolecular) · See more »

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.

Hydrogen bond and Lysine · Hydrogen bond and Salt bridge (protein and supramolecular) · See more »

The list above answers the following questions

Lysine and Salt bridge (protein and supramolecular) Comparison

Lysine has 160 relations, while Salt bridge (protein and supramolecular) has 30. As they have in common 4, the Jaccard index is 2.11% = 4 / (160 + 30).

References

This article shows the relationship between Lysine and Salt bridge (protein and supramolecular). To access each article from which the information was extracted, please visit:

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