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cysteine as a ruducer for ruduce the ORP ,on the other hand ,cysteine is not a essential for body
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What is Lcystien?
L-cysteine is a naturally occurring amino acid that is classified as a protein amino acid. One of the main functions of l-cysteine is the promotion of stomach lining health and also the correction of situations where the absorption of essential nutrients from food sources takes place. Many people are able to obtain as much of this protein source as they need without taking any type of supplement. L-cysteine can be found in a number of foods ranging from meats to dairy and vegetable sources. L-cysteine in the form of cysteine is found in many different protein sources. Chicken, turkey and pork are all good sources of cysteine. Even many varieties of processed luncheon meats contain this amino acid. Cooking does not destroy the presence of cysteine and in some cases may even help to enhance the absorption. When it comes to dairy products, l-cysteine as cysteine can be obtained from eggs and milk. Products such as ricotta and cottage cheese are also good sources. Plain yogurt and whey protein products also provide cysteine in a natural form. Onions, garlic, and broccoli are just a few of the vegetables that contain cysteine and provide good dietary resources when there is a need to augment l-cysteine levels in the body.
Disulfide bonds in a protein chain connect what?
Could depend on what your options are but out of my multiple choice answers this was the best:two cysteine residues.
What role does the ribosome?
They provide surface for protein synthesis.They are sites of protein synthesis
Why is cysteine unique among the amino acids?
Cysteine has a sulfide group attached to it and so can form very strong Di-sulfide bonds with other cysteine molecules.
Does the Golgi body play a major role in protein synthesis?
No. The Golgi bodies do not have a role. The main organelles involed in protein synthesis are the nucleolis, ribosomes, and mitochondria.
What type of macromolecule is cysteine?
Cysteine is an amino acid, which is part of the macromolecule protein.
What is Lcystien?
L-cysteine is a naturally occurring amino acid that is classified as a protein amino acid. One of the main functions of l-cysteine is the promotion of stomach lining health and also the correction of situations where the absorption of essential nutrients from food sources takes place. Many people are able to obtain as much of this protein source as they need without taking any type of supplement. L-cysteine can be found in a number of foods ranging from meats to dairy and vegetable sources. L-cysteine in the form of cysteine is found in many different protein sources. Chicken, turkey and pork are all good sources of cysteine. Even many varieties of processed luncheon meats contain this amino acid. Cooking does not destroy the presence of cysteine and in some cases may even help to enhance the absorption. When it comes to dairy products, l-cysteine as cysteine can be obtained from eggs and milk. Products such as ricotta and cottage cheese are also good sources. Plain yogurt and whey protein products also provide cysteine in a natural form. Onions, garlic, and broccoli are just a few of the vegetables that contain cysteine and provide good dietary resources when there is a need to augment l-cysteine levels in the body.
What does cysteine desulfurase catalyze?
From Wikipedia:In enzymology, a cysteine desulfurase (EC2.8.1.7) is an enzyme thatcatalyzesthe chemical reactionL-cysteine + [enzyme]-cysteine L-alanine + [enzyme]-S-sulfanylcysteine Thus, the two substrates of this enzyme are L-cysteine and [[[enzyme]-cysteine]], whereas its two products are L-alanine and [[[enzyme]-S-sulfanylcysteine]].This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include IscS, NIFS, NifS,SufS, and cysteine desulfurylase. This enzyme participates in thiamine metabolism.
What is the role of sulfur in human hair?
Hair is made of a type of protein called keratin. Keratin varies in exact composition and structure from species to species, but generally it contains large amounts of glycine, alanine, and cysteine. Cysteine is the one we're concerned about, because it contains a sulfur on the end of the side chain which can link up with the sulfur on another cysteine to form a disulfide bridge. These disulfide bridges help make keratin quite strong and insoluble in water.
What is the function of a caspase?
Caspases, also known as cysteine-aspartic proteases are a family or cysteine proteases that play an essential role in apoptosis, necrosis and inflammation. Capsases are essential in cells for apoptosis.
What is the significance of sodium-nitroprusside test?
This test is performed to test the presence of cysteine in the test solution (protein solution)
Which amino acid can stabilize protein structures by forming covalent cross-link between polypeptide chains?
cysteine
What is the percent composition of cysteine?
The percent composition of cysteine (C3H7NO2S) is: - C: 29,75 % - O: 26,43 % - H: 5,83 % - N: 11,57 % - S: 26,42 %
Disulfide bonds in a protein chain connect what?
Could depend on what your options are but out of my multiple choice answers this was the best:two cysteine residues.
What are 4 main elements in a protein?
Carbon, Hydrogen, Oxygen and Nitrogen. Sulfur is another as it is found in the amino acids cysteine and methionine.
What is cysteine milk?
cysteine is an amino acid which exists inside milk(also found in other places). it is important for its di-sulphide (s-s) bonds which are activated through heating (like pasteurization). it is an essential amino acid which the body needs to receive constantly, but meat is a more common source of cysteine for the body.
What has the author Mark W Robinson written?
Mark W. Robinson has written: 'Cysteine proteases of pathogenic organisms' -- subject(s): Cysteine proteinases, Cysteine Proteases, Pathogenic microorganisms, Eukaryota, Pathophysiology, Microbial enzymes, Enzymology, Viruses, Immunology, Chemistry, Bacteria
