Examples of using Polypeptide chains in English and their translations into German
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Colloquial
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Official
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Ecclesiastic
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Medicine
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Financial
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Ecclesiastic
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Political
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Computer
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Programming
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Official/political
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Political
Antibodies are also large and consist of four polypeptide chains.
There are four polypeptide chains held together by disulfide bonds.
It's a solid,it's a liquid it's a visco-elastic polymer made of polypeptide chains, but you eat it.
Polypeptide chains are composed of amino acids and can appear in alpha-helix or beta-sheet form.
It consists of three identical polypeptide chains and comprises three receptor binding sites.
The lectin has a molecular weight of 124 kDa andis composed of four identical polypeptide chains of 31 kDa.
All these types are made up of three polypeptide chains coiled together in the form of a triple helix.
These polypeptide chains of amino acids can be shaped as helixes or sheets, which come together to form a 3D structure.
An example of a chaperone is Hsp70, which binds to un-folded polypeptide chains and prevents aggregation.
Amino acid synthesis, polypeptide chains. transfer RNA, genetic code, enzyme expression. enzyme phosphorylation.
They have a similar basic structure comprising of four polypeptide chains held together by disulfide bonds.
During the process of protein formation the amino acids are linked in a long chain called polypeptide chains.
The CD3 molecule consists of five different polypeptide chains with molecular weights ranging from 16 to 28 kD.
Translation of mRNA involves 3 important steps- initiation,elongation, and termination, leading to the formation of polypeptide chains. Protein folding.
The cytochrome b-c1 complex(Complex III), has 11 polypeptide chains and functions as a dimer, and is also known as coenzyme Q.
The more there are hydroxyproline and hydroxylysine, segregating, following the synthesis of polypeptide chains, at the expense of proline.
Having deduced the presence of polypeptide chains, Astbury continued to pursue his pioneering studies of their configurations in fibrous proteins.
Homo-trimers generally consist of three individual, yet identical polypeptide chains, which form one structural unit.
In this final step, the polypeptide chains or random coils formed during translation fold into a 3D structure giving rise to a functional protein.
Because a hydrogen bond can be formed and formed,giving the opportunity to connect polypeptide chains in the beta-layer and in the alpha-helix.
Once the proteins are formed in their rudimentary forms of long polypeptide chains, they undergo several chemical reactions to form the final three dimensional structures of proteins.
The former binds strongly to the proteins and gives them a high negative chargewhilst the latter frees sulfhydryl groups, thus yielding polypeptide chains carrying an excess negative charge and similar charge to mass ratio.
As a consequence,TNFSF proteins only show biological activity when their three polypeptide chains are correctly assembled forming one receptor-binding domain(RBD), which in turn binds three receptors.
Chaperones are a family of proteins thatbind to unfolded proteins preventing aggregation of polypeptide chains with hydrophobic regions and ensuring that the correct conformation is obtained.
It is determined that not all polypeptide chain spiralized completely.
The isolation also prevents the polypeptide chain from aggregating into clumps with other chains within the cytoplasm.
Each amino acid within this polypeptide chain has a different property.
In IPMS this mechanism islocated in the last 120 amino acids of the polypeptide chain.