Examples of 'disulfide bonds' in a sentence
Meaning of "disulfide bonds"
Disulfide bonds are strong chemical bonds between sulfur atoms that stabilize the structure of proteins. They form when two cysteine amino acids come close together and their sulfur atoms react to form a covalent bond. Disulfide bonds play a crucial role in maintaining the three-dimensional shape and stability of proteins, and their presence or absence can greatly influence protein function and biological activity
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- plural of disulfide bond
How to use "disulfide bonds" in a sentence
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disulfide bonds
Disulfide bonds are formed by an interfacial process as follows.
Four conserved cysteines are involved in disulfide bonds.
Disulfide bonds cleave more rapidly at higher temperatures.
Provides for a greater recovery of disulfide bonds.
Disulfide bonds are displayed as ball and stick models.
Green tubes mark the disulfide bonds.
Each disulfide bonds was introduced orthogonally.
Thioglycolate depilatories work by hydrolyzing disulfide bonds.
Disulfide bonds in the correct position.
Localization of disulfide bonds by mass spectrometry.
It has nothing to do with disulfide bonds.
The formation of disulfide bonds requires an oxidative environment.
Two of the peptides are joined by two disulfide bonds.
The disulfide bonds are essential for biological activity.
The postulated disulfide bonds are shown.
See also
This can be achieved by reducing the disulfide bonds.
Selective reduction of disulfide bonds in proteins is also common.
Compact toxin protein structures are stabilized by disulfide bonds.
Disulfide bonds are broken.
It is assumed that all cysteines are engaged in disulfide bonds.
There are two disulfide bonds on each of the active polypeptides.
The amount is determined in consideration of generation of disulfide bonds.
Reduction of disulfide bonds by stannous ions is a relatively slow reaction.
Many extracellular proteins of eukaryotes contain disulfide bonds.
Proteins comprising disulfide bonds are oftentimes difficult to express recombinantly.
Cys participates in formation of disulfide bonds.
Among covalent bonds disulfide bonds are likely most important.
These chains are interconnected by disulfide bonds.
Disulfide bonds can also help stabilize the tertiary structure.
These two regions are linked by two or three disulfide bonds.
Intramolecular disulfide bonds can significantly contribute to the stability of proteins.
Cysteine is excluded because of its liability to form disulfide bonds.
Proteins without disulfide bonds may also be refolded as described herein.
The peptides of the invention optionally have no disulfide bonds.
Full reduction of the disulfide bonds eliminates lysozyme enzymic activity.
Periplasm expression enhances folding of proteins with disulfide bonds.
Preferred are disulfide bonds.
Cysteine residues are necessary to provide the covalent disulfide bonds.
Disulfide bonds are indicated.
Certain such polypeptides will have fewer disulfide bonds.
Disulfide bonds are analogous but more common than related peroxide.
Each chain also contains four intrachain disulfide bonds.
The formation of disulfide bonds by an interfacial process proceeds as described above.
It contains five cysteines which are not involved in disulfide bonds.
Hair strength is a function of the disulfide bonds between cystine molecules.
These individual chains are held together by several disulfide bonds.
This effects covalent disulfide bonds between the two partners.
Epitope peptides can also be attached to polyelectrolytes vía disulfide bonds.
A method using dithiothreitol to reduce disulfide bonds in the antibody fragment.
The reference is focused on cysteines involved in intramolecular disulfide bonds.
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Examples of using Disulfide
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The black disulfide is the main mineral
Four conserved cysteines are involved in disulfide bonds
A disulfide bridge may be intrachain or interchain bridge
