Übersetzung für "Disulfide bond" in Deutsch

Oxidation of the disulfide bond can occur here as well, with formation of sulfinic acid thioesters.

Under strongly denaturing conditions the protein is unstable in this form and tends to denature i.e. to lose its stable three-dimensional structure and the energetically favourable disulfide bond.

After reduction of the disulfide bond, for example with dithioeritrol, the labelled molecules can be washed off from the surface of the solid phase at a suitable pH value or ionic strength or with the addition of detergents.

Sodium/liquid ammonia, zinc/acid or phosphonium iodide are preferably suitable for reductive cleavage of the disulfide bond.

The dissociation of the VLPs preferably proceeds in the presence of a disulfide-bond-cleaving reducing agent and a Ca 2+ -ion-binding complexing agent.

In cases where toxicity is particularly critical, disulfide-bond-cleaving reducing agents to be preferred are 2-mercaptoethanol (2-ME) and monothioglycerol.

In accordance with the invention, directly bound means that the two proteins are covalently bound to one another, for example via a peptide bond or a disulfide bond.

The reason for this sensitivity is that the characteristic disulfide bond in the strained five-membered ring in the lipophilic chain of the molecule can be cleaved extremely easily.

Cyclic polypeptide for use according to one of claims 1 to 4, characterized in that the cyclic ring includes a disulfide bond between two cysteine amino acids.

When two cysteines are brought into close proximity in the tertiary structure, an enzyme called "protein disulfide isomerase" forms a disulfide bond between the two SH groups.

Due to the nature of the disulfide bond, it can be considered to be part of the primary structure of proteins, i.e. the polypeptide.

The modifications include glycosylation, formation of disulfide bonds, and phosphorylation.

The chains are usually linked to one another via disulfide bonds.

An important step in protein folding is the formation of disulfide bonds.

Because bacteriophage tail proteins are synthesized in the cytoplasma, it is not reckon with disulfide bonds.

Two molecules also the lively reduced glutathione-condensation of the disulfide bonds, are oxidized glutathione.

There are four polypeptide chains held together by disulfide bonds.

Hereby the disulfide bonds of the proteins are irreversibly broken up and the optimal unfolding of the tertiary structure is obtained.

Thiolated polymers can tightly bind to glycoproteins in the intestinal mucus layer by forming strong disulfide bonds.

Because of the disulfide bonds within such structures, the advantages of the invention have a particularly strong effect.

Preferred covalent bonds are, for example, amide, ester, thioester, ether, thioether and disulfide bonds.

Sulfhydryl groups are involved in disulfide bonds.

The invention concerns a process for increasing the formation of the natural protein conformation when disulfide-bonded proteins are secreted by a prokaryotic host organism that contains a recombinant DNA coding for the secreted protein whereby the host organism is cultured in a suitable culture medium under suitable conditions for the expression of the recombinant DNA, which is characterized in that a culture medium containing 0.1 to 20 mmol/l of one or several thiol reagents is used.

The keratin-reducing substance cleaves some of the disulfide bonds of the keratin to --SH groups, so that the peptide network is loosened and the keratin structure is reoriented under the strain applied to the hair by the mechanical shaping treatment.

A process for increasing the formation of the natural protein conformation when disulfide bonded proteins are secreted by an E.coli host that contains a recombinant DNA coding for the secreted protein, comprising culturing the host in a suitable culture medium in the presence of oxygen under conditions suitable for the expression of the recombinant DNA, wherein said culture medium contains 0.1 to 20 mmol/l of one or more thiol reagents.

The hair is then brought into a new shape and subsequently fixed in the new shape by treatment with a suitable oxidant, with concomitant rebonding of the previously split disulfide bonds.

After the required reaction time of the hair shaping agent the rolled hair is rinsed with water and with a watery solution of an oxidation substance, preferably with a 2% hydrogen peroxide solution by reestablishing the previously cracked disulfide bonds of the hair keratin and is then fixed in the new shape.

Furthermore, all the proteins contained in the factor XIII-containing solution can, by reason of a lower reactivity toward free mercapto groups or as a consequence of a behavior in the subsequent elution which differs from that of factor XIII, be separated from factor XIII using an agent which reduces the disulfide bonds.

Because the "b" subunits themselves do not have free mercapto groups, on the contrary all the SH groups provided by cysteines being in the form of disulfide bonds within the "b" subunits, they do not bind to the carrier matrix and can be removed by washing.

There is a problem with the reduction of potentially free thiol groups to free reactive thiol groups, if in addition also the conformation-determining disulfide bonds are broken up and thus the nativity of the proteins is lost.

The processing step must, however, be carried out under conditions in which the conformation stabilizing disulfide bonds are retained as far as possible, since otherwise the latter could also, i.a., be cleaved to thiol groups and could also be nitrosated in the subsequent reaction.