Biochemistry : Previous Year Questions

Chapter 1: Protein Chemistry

Q. What is peptide linkage? Explain the partial double bond nature of peptide linkage.

Q. Explain rretrival pathway of resisdential ER protein back to ER.

-Q. Derive henderson and ahsselbalch equation and give its application in buffer preparation.

Q. Explain bicarbonate bugger system.

Q. Explain concept of buffer, strength of buffer and buffer value.

Q. Describe classification of amino acid.

Q. In what order will following amino acid elute from a dowex -50 column at ph 3.2 alanine (pl=6.02), arginine (pl=10.76), glutamic acid (pl=3.2), serine (pl=5.68), and tryptophan(pl=5.88)?

 Q. Explain the role of signal Recognition particle in transfer of protein to the E.R. membrane.

Q. Explain Anomers and Epimers of Glucose.

Q. Give two epimers of glucose with strcuture.

Q. Wha are tautomers? Give their implications  in pairing of bases.

Q. What is quaternary structure of proteins? Exolain with suitable example/

Q. Explain the secondary structure of protein with examples.

Q. Describe the classification and Nomenclature of fattyacid

Q. What are phosphoglycerid ? Give major classes of phosphoglycerides with their function.

Q. Draw structure of tryglyceride and enlist the functions.

Q. Explain nomenclature and classification of fatty acid.

Q.  Justify:-Membrane lipids comprise phospholipids.

Q. Describe the structure and function of phospholipids.

Q. How are lipids classified on the basis of their chemical structure?

Q.  Justify : ‘Amino acids and proteins can act as buffers’

Q. What is the intracellular and extracellular buffering system used by animals with lungs?

Q. Explain in brief the secondary structures encountered in proteins.

Q. Explain the term cot curves and give their significance

Q. Giving suitable examples explain the terms enantiomers and epimers.

Q. What are reducing sugars? Describe any one method for estimation of reducing sugars.

Q. Explain C- terminal sequencing of protein by giving at least two methods..

Q.  Is it possible to separate amino acids by the above mentioned method? eletrophoresis

Q.  Explain the targeting of secretory proteins to ER.

Q. Justify, non covalent interactions are crucial to macromolecular structure and function.

Q. Diagrammetically illustrate the d series of aldoses.

Q. Enlist various types of isomerism observed in sugars and eexplain any one type with example.

Q. What are steroids? Explain structure and function with suitable example.

Chapter 2: Biochemistry and Molecular Biology techniques

Q. Explain the z form of DNA.

Q. How does stereo chemistryu affects interactions of organic molecules.

Q. Explain why RNA, not DNA is hydrolyzed under basic PH conditions? What is global charge of trinucleotide APGpUpC at neutral pH.

Q. Explain significance of folic acid in cellular biosynthesis.

Q. Explain coenzyme form of folic acid. Explain its functio.

-Q. Diagrammatically illustrate working of confocal microscope, comment on its application.

Q. Diagrammatically illustrate double helix of DNA showing Watson and Crick base pairing

Q. Explain acid-base catalysis with suitable example of enzyme

Q. Explain charge transfer complex in molecules.

-Q.Explain metal-ion catalysis of enzyme.

Q. Explain principle and application of immunoelectron microscopy.

Q.  Explain the mechanism of substitution reaction giving suitable examples.

Q. A mixture of following amino acids is subjected to electrophoresis at pH 3.9: Ala, Leu, Arg, Asp, His. Which ones will go toward anode (-)? Toward cathode (+)? Why?

Q. What is hydrogen bonding? Explain the significance of H-bonding in biomolecules.

-Q. What are terpenes? Comment on their biological roles.

Chapter 3: Developmental Biology

Q. Write short note on :- organizers in drosophila.

--Q.  Explain the gastrulation process in drosophila.

Q. Explain the role of morphogen gradients in Drosophilla

Q. Justify: ‘Maternal messenger RNAs are critical to the formation of the anterior-posterior axis in Drosophila’

Q. Diagrammatically illusttrate the antirio posterior body axis formation in drosophila.

Q. Justify, although RNA is signle stranded it can possess extensive secondary structure.

Q. Compare structure of mRNA of bacteria and eukaryotes.

Q. Diagrammatically illustrate the process of gastrulation in Xenopus

Q. Q. Describe the process of blastulation in Xenopus embryo.

-Q. Describe organizers in xenopus.

Q.  Explain host-guest interaction and comment on its applications in biology

Q. Explain the role of MPF in development

-Q.Explain the process of commitment during developmental process.

-Q. Explain mutarotation with suitable example..

Q. Explain biochemical significance of inductive effect.

Q. WRite a note on immunoelctron microscopy.

Q. What is difference between configuration and conformation of biomolecule ,explain with example.

Chapter 4: Cell Biology

-Q. Write a short note on Apoptosis.

Q. Describe cell cycle and diagrammatically represent the check points of cell cycle.

Q-. What is meant by dedifferentiation and redifferentiation. Explain giving suitable example.

Q. Describe the structure and function of golgi complex.

Q. Describe structure and function of golgi apparatus.

Q. Justify that mitochondria plays a significant role in apoptosis. 

Q.  Describe the structure and function of microtubules.

Q.  Describe the structure and function of microfilaments.

Q. Justify: ‘The cyclin-cdk complexes play important role in regulation of cell cycle’.

Q.explain the intermediate filament structure and function.

Q. Describe regulation of cell cycle in eukaryotes.

Q.  Explain the stages of commitment.

Q.  Justify: ‘Myxobacteria produce various signaling molecules during fruiting body formation’.

-Q. Describe cell-cell signaling in myxobacteria.

Q. Explain life cycle of myxobacteria.

Q. Describe the process of blastulation in Xenopus embryo.

Q. Draw structure of Riboflavin and explain its biochemical mechanism in metabolism.

Q. Enlist the coenzyme forms of riboflavin and explain their role in enzyme catalysis with suitable examples.

--Q. Describe structure and functions of vitamin K.

Q. Describe structure and function of vitamin A.

Q. Desscribe structure and function of vitamin E.

Q. Explain UV induced changes in viamin D.

Q.  Explain biochemical role of copper and molybdenum in enzymic reactions.

-Q. Explain addition reaction with examples.

-Q. What is qorum sensing? Discuss its role in virulence of pathogenic bacteria.

--Q. Explain quorum sensing in Gram Negative Bacteria.

Q. Explain quorum sensing in Gram Positive Bacteria..

-Q.Explain applications of Biofilm in pathogenises.

--Q. Describe the mechanism of biofilm formation with suitable example./significance

-Q.  Describe the life cycle of Dictyostelium/ cellular diffferentiation in it.

Q.Explain molecular mechanism of quorum sensing in Myxobacteria and lifecycle of it.

Q.  Describe the function of Molybdenum and Nickel as cofactor

Q. Explain function of iron as cofactor.

Q. Describe function of manganese and zinc as co factor.

-Q. Describe role of copper as co factor.

Q. Explain NAD as co factor and any two biochemical reaction.

Q. Write a note on hox code