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Jlenok [28]
3 years ago
14

What is the content of theinjected material (vaccine)?​

Biology
1 answer:
krok68 [10]3 years ago
8 0
Aluminium, an adjuvant.
MF59 (squalene oil), an adjuvant.
Thiomersal, also called Thimerosal.
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What term describes the specific genetic makeup or code for an organism?
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What characteristic of cardiac muscle causes contraction of the heart as a unit?
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1. For this task, you will imagine that you are a reporter for a scientific magazine. Your task is to explain the process of pro
JulijaS [17]
All cells as we can say they work through their proteins. The work of proteins is being characterized by their sub-atomic capacity, contribution to a specific natural process and limitation inside. Segments of protein work which are being characterized by the correct synthesis, adaptation of proteins and structure which are being scrambled in the DNA area which is another name is called locus encoding the protein.
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It leaves the core and goes straight to the cytoplasm. mRNA interferes with cell structure referred to as ribosome and fills in as cells contrasting agent within the procedure of protein union. Ribosome comprises of ribosome RNA particles or rRNA and proteins which are sorted out into two subunits.
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3 0
3 years ago
Select the true statements about protein secondary structure.
saul85 [17]

Answer:

C.The β‑pleated sheet is held together by hydrogen bonds between adjacent segments.

Explanation:

Hello!

The most common secondary structures are α-helix and β-sheets. The structures are defined by regular hydrogen bonds formed between the N-H and C=O groups of the amino acids that form the chain. These structures form in segments of the protein as an intermediate before it folds into the 3D tertiary structure.

<u>α helix  </u>

It is a cylindrical structure that comprehends a helical backbone, while the side chains extend outward in a helical distribution. The α-helix stabilizes through hydrogen bonds between the amines and carbonyls groups of the backbone. Each carbonyl group forms a hydrogen bond with the amine group four residues later in the main chain. Thus, except for the amino acids near the end of the α-helix, all the carbonyls and amines groups in the main chain are linked by hydrogen bonds. Each residue corresponds to a translation of 1,5Ǻ and a turn of 100º this equals 3,6 residues per turn.

From the observer point of view, if the rotation of the helix is clockwise or right-handed, it's called dextrorotation and if the rotation is counterclockwise or left-handed it's called levorotation. Dexorotation or dextrogyre is the most common rotation of α-helixes in proteins. Levorotation or levogyre is very rare but can be found in proteins with a large content of achiral glycine.

<u>β-sheets (β-pleated sheets) </u>

This structure consists of at least two β-strands (polypeptide chains), the strands conform a backbone of three to ten amino acids in an extended formation that connects laterally with hydrogen bonds. The distance between adjacent amino acids in a β-strand is approximately 3,5Ǻ in contrast to the 1,5Ǻ distance of an α helix. The chains that form a β-sheet have directionality conferred by their N-terminus and C-terminus. Adjacent β-strands can form hydrogen bonds in antiparallel, parallel or mixed arrangements. In the antiparallel arrangement, the adjacent strands are said to have opposite directions (N-C vs C-N) this allows the bonds to be established between the amines and carbonyls groups of each amino acid with the carbonyls and amines of the adjacent amino acid. This way the bonds between carbonyls and amines are planar, which allows strong interstrand stability.

In the parallel arrangement, the adjacent strands have the same direction (N-C vs N-C). In this type of arrangement, each amine forms a hydrogen bond with the carbonyl of the adjacent amino acid, but its carbonyl group forms a hydrogen bond with the amine group of the amino acid two residues later.

I hope you have a SUPER day!

6 0
3 years ago
Read 2 more answers
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