“The most important structure of a protein is its tertiary structure everything else doesn’t matter” Based...
“The most important structure of a protein is its tertiary structure everything else doesn’t matter” Based on your understanding of protein structure can you argue both for (2.5 points) and against this statement (2.5 points)
Homework Answers
Protein is the most essential component of the body. It is made up of primary secondary and tertiary structure. Primary is simplest amino acid chain joined by poly peptide bond. For example hormone insulin has two poly peptide chains. Secondary structure is local fold structure form within poly peptide because of the interaction in the atom of polypeptide. Tertiary structure is mainly because of the interaction between R group of amino acids and it is the overall three dimensional structure of protein.
“The most important structure of a protein is its tertiary structure everything else doesn’t matter” is true as the function of protein depend on the tertiary structure. When protein get denatured by the exposure of over heat and high acid it get denatured and protein become non-functional. When a protein loses its tertiary structure, but not its primary sequence, it is said to be denatured. Denatured proteins are usually non-functional. Hence we can say that The most important structure of a protein is its tertiary structure everything else doesn’t matter.
“The most important structure of a protein is its tertiary structure everything else doesn’t matter” is not true as because tertiary structure of protein can not form without primary and secondary structure. These two structure plays the role of backbone of tertiary structure. Some protein in the body are present in these structure only like insulin.
Without primary structure denatured protein can not retain its original structure. Primary structure provide stability by making tertiary structure in the case of denaturation. Hence we can say that the statement “The most important structure of a protein is its tertiary structure everything else doesn’t matter” is not true.
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“The most important structure of a protein is its tertiary
structure everything else doesn’t matter” Based...
List and describe the two approaches to determining the tertiary structure of a protein. Experimental Determination...
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What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges...
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges In a hydrolysis reaction, B) hydrophilic interactions A. an acid reacts with an alcohol. C) disulfide bonds E. an este reacts with NaOH. C. anester reacts with H.O. D) peptide bonds D. an acid neutralizes a base. E) hydrophobic interactions E. water is added to markene. . All amino acids have chiral Carbon atoms except a. Val 6. Lys C. ASP d. Ala e....
question 3: what happens to the structure of a protein when it is denatured? question 4:...
question 3: what happens to the structure of a protein when it is
denatured?
question 4: why is it important for a protein to be at a
certain ph to carry out its function
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6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein...
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The Kjeldahl method is the most widely used method for determining the protein content of foods....
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The small monomeric G protein Ras is an important component of most receptor tyrosine kinase signaling...
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please only do H-M. i have done everything else. 2. During the acid catalyzed polymerization of...
please only do H-M. i have done everything else.
2. During the acid catalyzed polymerization of terephthalic acid and ethylene glycol, some fraction of methanol (CH-OH) is incorporated, but no more ester bonds can be formed. a. Based on the above, what is the extent of reaction, p? b. How does fav determine whether a linear or network polymer is formed as p nears 1? c. Why do you believe the polymer in this reaction will be a gel-network or...
Problem #2 [50 Points, 10 each) A structure has the stresses on its most critical point...
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List and describe the two approaches to determining the tertiary structure of a protein. Experimental Determination Computational prediction There are three methods of computational structure prediction. Define each of the methods and describe when each method would be used. There are three types of helices formed by the secondary structure of protein. List three helices and rate how tightly coiled they are. Explain your reasoning. Choose any three of the twenty amino acids. Based on what you know about the...
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges In a hydrolysis reaction, B) hydrophilic interactions A. an acid reacts with an alcohol. C) disulfide bonds E. an este reacts with NaOH. C. anester reacts with H.O. D) peptide bonds D. an acid neutralizes a base. E) hydrophobic interactions E. water is added to markene. . All amino acids have chiral Carbon atoms except a. Val 6. Lys C. ASP d. Ala e....
question 3: what happens to the structure of a protein when it is
denatured?
question 4: why is it important for a protein to be at a
certain ph to carry out its function
zymes in your textbook, especially the sections on enzym REPORT: Your report should include two separate files: a table of the data from your enzyme experiments online and conclusions consisting of answers to the questions. WARM-UP QUESTIONS: 1. What part of the name 6-O-a-L-ramnosyl-D-glucosidase shows that...
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein - that is, its overall shape and how the chains are "folded” around each other - is very important for its function. In an aqueous environment, in an active, folded state the hydrophilic amino acids in the protein are facing outwards exposed to the water and the hydrophobic amino acids are hidden away from the water in the core of the protein. In a...
The Kjeldahl method is the most widely used method for determining the protein content of foods. It is based on the fact that protein is the only macronutrient (major nutrient) that contains nitrogen. The method gives the value of g of nitrogen per 100 g of food. That value is then multiplied by a constant, 6.25 g protein per g of nitrogen, to give the result expressed as g of protein per 100 g of food. a. Explain why this...
The small monomeric G protein Ras is an important component of most receptor tyrosine kinase signaling pathways. It can regulate a number of downstream signaling components, perhaps most famously the MAPK cascade. Unlike other monomeric G proteins that we have discussed previously in class, Ras is anchored at the plasma membrane by a covalently bound lipid anchor. If Ras was specifically mutated so that it did not get this lipid modification (but was otherwise completely unchanged), what do you hypothesize...
Most commonly known for its ability to bind to oxygen, iron also plays the important role of acting as a cofactor oxidation-reduction reactions. to many enzymes in numerous Red blood cells without iron become pale and this is called hypochromic. In individuals with lighter skin, this also results in a distinct pale appearance called_pallor . Vegans, vegetarians, and those following a variety of plant-based diets can get enough iron from their diet from eating foods that contain chloro- iron along...
please only do H-M. i have done everything else.
2. During the acid catalyzed polymerization of terephthalic acid and ethylene glycol, some fraction of methanol (CH-OH) is incorporated, but no more ester bonds can be formed. a. Based on the above, what is the extent of reaction, p? b. How does fav determine whether a linear or network polymer is formed as p nears 1? c. Why do you believe the polymer in this reaction will be a gel-network or...
Problem #2 [50 Points, 10 each) A structure has the stresses on its most critical point (a) as shown. If the yield strength for the material is Sy=420 MPa. Determine the following 1. Draw Mohr's Circle for the stress element 2. Principal Stress element showing all stresses and angle 3. Maximum Shear Stress element showing all stresses and angle 4. Determine the factor of Safety of this structure against yielding. 5. If the structure fails, what would you do to...
Consider an important protein like beta-galactosidase, which breaks down lactose. Many bacterial species have beta-galactosidase. But that doesn't mean that the amino acid sequence of beta- galactosidase in all those bacterial species is exactly the same. Far from it. As bacteria diversified into different species over evolutionary time, beta-galactosidase encoded in the genomes of the bacteria also diversified. However, we can assume that even though beta-galactosidase diversified, it was under pressure to maintain structure and function, because the reaction it...
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