Sentences with phrase «cysteine bonds»

What follows should be regarded as a very rough calculation that relies on several unproven assumptions, including the following: a) that the researchers» hypothesis that the glutamyl - cysteine bonds are in fact responsible for the glutathione - boosting power of whey protein is true, b) that the total body increase in glutathione was similar to the increase seen in the tissues the researchers measured, and c) that raw, undenatured whey protein produces a similar response in people as it produces in mice.

Raw egg whites contain a similar concentration of the unique glutathione - boosting glutamyl - cysteine bonds.

These two proteins contain unique glutamyl - cysteine bonds that resist digestion and enter the blood stream in tact.

Alpha - lactalbumin is the other major whey protein, but it doesn't contain any glutathione - boosting glutamyl - cysteine bonds.

Not exact matches

Most commonly bonds are made between two cysteines to stabilize protein structure, but if a free cysteine is present, as in G12C K - Ras, a specifically designed drug can form a bond to the cysteine.

In a hair strand, the keratin molecules are mainly held together by two forces: chemical cross-links between cysteines (a type of amino acid) and weaker hydrogen bonds.

They bond with a cysteine amino acid which only occurs in JAK3 — thereby blocking this enzyme but not the other Janus kinases.

These findings suggest that animal cells may have fail - safe mechanisms that prevent the surface expression of improperly folded proteins with unpaired or improperly bonded cysteine residues.

They carefully chose two spots to mutate so that the cysteines on opposing chains would covalently join and two of the three chains would be held together by a disulfide bond.

We and others have reported that FP cysteine residues form inappropriate disulfide bonds in the secretory pathway (Figure 1)[4,6 — 8].

Homocysteine and homocystine can attack an exposed disulfide bond or cysteine residue, respectively, on proteins to form cysteine - homocysteine mixed disulfides, which may lead to the functional inactivation of the protein.

Thioester bonds reversibly with the cysteine on the peptides to form thioester peptide nucleic acid (tPNA).

This form is cystine and is comprised of two cysteines joined together by a disulfide bond.

This bonded cysteine is also found in human breast milk, and can be replicated with raw cow's milk in the form of undenatured whey protein.

Mainly because it contains a very stable and potent form of cysteine: covalent bonded cysteine and not the denatured cystine that can occur in highly processed dairy.

Cysteine, by virtue of its ability to form disulfide bonds, plays a crucial role in protein structure and in protein - folding pathways.»