1 mark Questions
1. Natural form of subtilisin enzyme is inactivated by bleach in detergents. How?
2. How BCAA are useful for athletes?
3. What are esssential amino acids?
4. What are epitopes?
5. Explain with an example the therapeutic uses of whey protein
6. Which technique did Linus Pauling and G.N. Ramachandran use for studying the 3D shpe of proteins?
7. Name two organophosphates that are used as mosquito repellent.
8. Why sickle cell anemia is co-prevalent in malaria affected areas?
9. How does whey protein causes browning in breads, biscuits etc.
10.Why 2D gel electrophoresis is better than single dimension electrophoresis?
2 Mark Questions
1. Among the bio molecules, why do proteins have maximum diversity in functions?
2. How are H-bonds created in proteins and when are they strongest?
3. Why is sickle cell anemia called a molecular disease?
4. How is mass spectrometry useful in protein studies? Expand the term MALDI and ESI
5. How are hydrophobic interactions created in protein?
6. Name any four physical/chemical properties of enzyme which might be useful to change by site directed mutagenesis.
7. How are recombinant vaccines safer than conventional vaccines?
3 Mark Questions
1. Describe the important parts of a mass spectrometer with diagrams. Describe its uses in study of proteins.
2. Describe the technique used to identify sickle cell anemia in the laboratory. Who developed this technique?
3. In a variant of chymotrypsin Asp 102 is replaced by Glu 102. Do you expect the enzyme to retain activity? Schematically indicate the role of the amino acid residues participating in catalysis.
4. Subtilisin has been improved by protein engineering to serve as a component of laundry detergent. What are the features of this improvement and how have they been achieved?
5. Monoclonal antibody against CD3 is an effective therapeutic agent in overcoming renal graft rejection. Why?
6. Briefly explain how the serine residue in some enzymes can become acidic. Also suggest how you can confirm that a serine residue is involved in catalysis.
7. Nature has found a useful folding pattern in chymotrypsin. How does it help in hydrolysis?
8. Draw a neat and labelled diagram of MS. If a protein is having molecular weight 300000Da and charge on that is 3H+, then at what m/z ratio does this protein would be detected out?
9. Explain how charge relay system operates in chymotrypsin. Why is the broad specificity of chymotrypsin advantageous?
5 Mark Questions
1. Name any five protein based products and their uses.
2. What do you understand by the term nutraceutical? Name three sources of nutraceuticals and their uses?
3. Explain structural-function relationship with taking an example of chymotrypsin.
4. Explain O'Farrels technique in detail.
1. Natural form of subtilisin enzyme is inactivated by bleach in detergents. How?
2. How BCAA are useful for athletes?
3. What are esssential amino acids?
4. What are epitopes?
5. Explain with an example the therapeutic uses of whey protein
6. Which technique did Linus Pauling and G.N. Ramachandran use for studying the 3D shpe of proteins?
7. Name two organophosphates that are used as mosquito repellent.
8. Why sickle cell anemia is co-prevalent in malaria affected areas?
9. How does whey protein causes browning in breads, biscuits etc.
10.Why 2D gel electrophoresis is better than single dimension electrophoresis?
2 Mark Questions
1. Among the bio molecules, why do proteins have maximum diversity in functions?
2. How are H-bonds created in proteins and when are they strongest?
3. Why is sickle cell anemia called a molecular disease?
4. How is mass spectrometry useful in protein studies? Expand the term MALDI and ESI
5. How are hydrophobic interactions created in protein?
6. Name any four physical/chemical properties of enzyme which might be useful to change by site directed mutagenesis.
7. How are recombinant vaccines safer than conventional vaccines?
3 Mark Questions
1. Describe the important parts of a mass spectrometer with diagrams. Describe its uses in study of proteins.
2. Describe the technique used to identify sickle cell anemia in the laboratory. Who developed this technique?
3. In a variant of chymotrypsin Asp 102 is replaced by Glu 102. Do you expect the enzyme to retain activity? Schematically indicate the role of the amino acid residues participating in catalysis.
4. Subtilisin has been improved by protein engineering to serve as a component of laundry detergent. What are the features of this improvement and how have they been achieved?
5. Monoclonal antibody against CD3 is an effective therapeutic agent in overcoming renal graft rejection. Why?
6. Briefly explain how the serine residue in some enzymes can become acidic. Also suggest how you can confirm that a serine residue is involved in catalysis.
7. Nature has found a useful folding pattern in chymotrypsin. How does it help in hydrolysis?
8. Draw a neat and labelled diagram of MS. If a protein is having molecular weight 300000Da and charge on that is 3H+, then at what m/z ratio does this protein would be detected out?
9. Explain how charge relay system operates in chymotrypsin. Why is the broad specificity of chymotrypsin advantageous?
5 Mark Questions
1. Name any five protein based products and their uses.
2. What do you understand by the term nutraceutical? Name three sources of nutraceuticals and their uses?
3. Explain structural-function relationship with taking an example of chymotrypsin.
4. Explain O'Farrels technique in detail.
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