1. Ribonuclease. C.B. Anfinsen initiated and confirmed the nation that, acting in concert, the specific primary structure of a polypeptide and the innate properties of the side chains of its amino acids due to the polypeptide and it's biologically active that is tertiary structure, In 1972 R.C.B.Anfinesen got the Noble Prize for this definitive work.
Anfinsen identified four disulfide bridges in the ribonuclease protein, suggesting that the enzyme is highly folded. Almost all enzymes, their catalytic activity of ribonuclease maintenance of a particular three-dimensional shape of proteins. In concentrated solutions of beta-mercaptoethanol and urea, the disulfide bridges of the enzyme activity.
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The Enzyme is said to be denatured. If the beta-mercaptoethanol and urea are removed by dialysis and essentially many types of catalytic activity of the proteins is restored.
2. Haemoglobin. Hemoglobin is one of the fully sequenced proteins. We got the structure and function of hemoglobin as the outcome of 50 years of research by M.F. Perutz. He got the Noble Prize in 1962, along with J.C.Kendrew, for their studies of hemoglobin and myoglobin.
The hemoglobin is a conjugated globular protein, that is, it contains some non-protein part. Its secondary, tertiary, and quaternary structure is typical of all higher vertebrate hemoglobins. The protein part that is the hemoglobin that is called globin, proteins is composed of four polypeptide chains, and in this part's which is the globular shape. The 4 globin chains consist of 2 identical pairs of proteins:
(i) Two alpha chains
(ii) Two beta chains.
The non-protein portion of hemoglobin consists of four iron-containing haem groups, one associated with each of the four globin chains. Nineteen of the twenty biologically important amino acids are included in the globin of hemoglobin.
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A hemoglobin molecule is highly symmetric; it can be divided into two identical halves, each consisting of an alpha beta-dimer. The tetramer is a mildly flattened sphere having a maximum diameter of about 5.5-5.6 nm. The 4 polypeptide chains are arranged is not good chains have stabilizing interactions. A cavity about 2.6 nm long in length and varying in width from about 5 - 10 degrees passes along the axis. Protein's each globin chain envelops that is haem group in a deep cleft of proteins.
3.Immunoglobulines. The ability to resist infection by pathogens and by multicellular endoparasites is called immunity. Specific immune response functions by recognizing particular chemical structures, known as antigens- on the surface of invading cells.
These antigens interact with protein molecules produced by the host, the immunoglobulins, which blind the antigen in much the same way as an enzyme binds its substrate. Specific protein's immune responses involve the maximum types of cells. One type is B-lymphocyte or B- cell and is capable of producing free immunoglobulins that are called antibodies.
Do you know about proteins it is best for the skin?
No, we do not about proteins function for the skin.
Okay. Read carefully the below statement:
Protein that provides softness for Skin -We take a daily balanced diet and people give first priority of proteins but a maximum person does not complete knowledge of proteins. I told completely about proteins in the above statement then also discuss proteins. Protein's function in the body's muscle growth due to glowing our skin in the other way I can say that proteins that provide softness for skin in daily life due to it is best useful for the body.
How to dry seeds that are wet because of rain without losing their proteins?
We know about dry seeds in have not water and lackness of water so we eat dry seeds with wet seeds because 70% needs water for body dry food or seeds completely can not digest properly. all types of seeds found fully proteins that grow our body's muscles.
Without rain take dry seeds losing their proteins.
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