The history of Insulin

It shows how insulin was used and how it was discovered by whom and its problems and also how the problems where resolved so that human life could be better.

Reference:
PhajEjHmong8. 2012. The history of insulin. http://www.youtube.com/watch?v=PGXgQKX2EzQ. Accessed on 13th April, 2013.

Hemoglobin

Gives information on hemoglobin, what it is and it’s function.

Reference:

Khanacademy. 2010. Hemoglobin. http://www.youtube.com/watch?v=LWtXthfG9_M. Accessed 13th April, 2013.

The cell theory

It explains how the cell theory came about and gives a little history on the scientists.
Scientific discovery isn’t as simple as one good experiment. The weird and wonderful history of cell theory illuminates the twists and turns that came together to build the foundations of biology.

Reference:
Royal-Woods Lauren , Augenblick Studioeference.2012.The wacky history of cell theory. http: http://www.youtube.com/watch?v=4OpBylwH9DU. Accessed on April 13th, 2013.

Enzymes MCQ

Have a go its only 10 questions

1. What are enzymes?

A. Biological catalyst that speed up chemical reactions by providing an alternate pathway of higher activation energy

B. Any molecule that speed up chemical reactions by providing an alternate pathway 

C. A biological molecule that slows the rate of reaction

D. An alternate pathway

E. Biological catalyst that speed up chemical reactions by providing an alternate pathway of higher activation energy

2. What are the three distinctive features of an enzyme:

1. Catalytic power

2. Specificity 

3. Alternate

4. Regulation

A. 1,2,3 and 4 only

B. 1 and 2

C. 1 only

D. 2 and 3 only

E.1, 2 and 4 only

3. The highest energy arrangement of atoms that is intermediate in structure between the structure of the reactants and the structure of the products is the 

A.Free Energy

B.Transition state

C.Catalyst

D.Enzyme

E. Activation energy

4. Which one best describes activation energy?

A. Low energy

B. The minimum amount of energy for the reaction to occur

C. The maximum amount of energy for the reaction to occur

 D. The energy for a reaction

E. A different pathway

5. In mixed inhibition where does the inhibitor bind?

A.Substrate active site

B. Enzyme active site

C. To the substrate

D. Same site as the subastrate

E. Free enzyme or Enzyme- substrate complex

6. Which Lineweaver-Burk plot is for mixed inhibition?

 

A.

B. C. 

D.

E. 

 

7. What increase the rate of reaction but denatures the enzyme as well?

A. Substrate concentration

B. Enzyme concentration

C. Temperature

D. Time

E. Speed

8. Increasing substrate concentration increases the rate of the reaction until the enzyme’s active site becomes __________ .

A. Saturated

B. Active

C. Slow

D. Fast

E. Inhibited

9.In which type of inhibition does the inhibitor bind to the enzyme’s active site?

A. Non-Competitive 

B. Mixed 

C. Uncompetitive

D. Competitive

E. All of the above

10. Non-Competitive inhibition cannot be overcome by increasing

A. Temperature

B. Substrate concentration

C. Enzyme concentration

D. pH

E. Volume 

Glycolysis

Glycolysis jigsaw puzzle game

 

To solve the glycolysis puzzple follow the link below.

<div style=’font-size:10px; font-family:Arial, Helvetica, sans-serif; color:#000;’><a href=’http://www.proprofs.com/games/jigsaw/glycolysis-2/&#8217; target=’_blank’ title=’Glycolysis jigsaw puzzle game’>Glycolysis jigsaw puzzle game</a> » <a href=’http://www.proprofs.com/games/jigsaw/&#8217; title=’free online jigsaw puzzles’ target=’_blank’>free online jigsaw puzzles</a></div>

Enzymes

To play the Enzymes Hangman game, follow the link below…and have fun while learning!

<div style=’font-size:10px; font-family:Arial, Helvetica, sans-serif; color:#000;’><a href=’http://www.proprofs.com/games/word-games/hangman/enzymes-1/&#8217; target=’_blank’ title=’Enzymes hangman game’>Enzymes hangman game</a> » <a href=’http://www.proprofs.com/games/word-games/hangman/&#8217; title=’make hangman’ target=’_blank’>make hangman</a></div>

Past Paper 2

REFERENCE:

University of Kerala. 20th October, 2013.Kerala,India. http://www.keralauniversity.ac.in/index.php/component/content/article/29-the-cms/316old-question-papers-of-bsc-biochemistry.html. Accessed on 12th April,2013.

 Most the question below are relevant to Biochemistry and it helped as a revision past paper.
B.Sc. Supplementary Degree Examination, August 2009
Part – III : BIOCHEMISTRY (Main)
Paper – II : General Biochemistry
Time : 3 Hours Max. Marks : 55

PART – A
Answer any ten questions. Each question carries 2 marks.

1. List the organelles in an animal cell.

2. What is a Stereoisomer ?

3. How will you generate glucosazone ?

4. What are hetero polysaccharides ? Give two examples.

5. List Vit-B compounds.

6. Explain Iodine number.

7. How are Prostaglandins and Leukotrienes formed ?

8. What is optical activity of a compound ?

9. Write the structure of glutathione.

10. What enzymes and conditions will you use to hydrolyze proteins ?

11. Identify factors contributing to secondary structure of proteins.

12. What are lipases ?

13. What is meant by annealing ?

PART – B
Answer any three questions. Each question carries five marks.

14. Discuss the products of arachidonic acid metabolism.

15. Identify the differences between glycoproteins and proteoglycans.

16. Write the steps in the synthesis of a sample peptide.

17. Write on DNA double helix.

18. Write on the significance of Km and Vmax. (3×5=15 Marks)

PART – C
Answer any two questions. Each question carries ten marks.

19. Discuss on the factors affecting enzyme function.

20. How will you purify a protein and determine its aminoacid composition ?

21. Compare the mode of action of penicillin, streptomycin, tetracycline andchloramphenical antibiotics. (2×10=20 Marks)

——————————

Past Paper 1

REFERENCE: Department of Biology. 03rd March,2013.University of York, Wentworth Way,               York,YO105DD,UK.http://www.york.ac.uk/biology/intranet/currentundergraduatestudents/common-pages/past-papers/. Accessed on 12th April,2013.

THE QUESTIONS BELOW WHERE THE ONES RELEVANT TO OUR COURSE

These question help me to review most of the topics covered in Biochemistry and it also guided me towards how much information I need to write to be awarded the assigned marks.

3. From the amino acid sequence shown below:

NLVETSGPCK

a) Choose the two amino acids with the most hydrophobic (non-polar) side-chains

and provide the names of the amino acids. (2 marks)

(i)

(ii)

b) Choose two amino acids that could participate in a salt-bridge interaction with

each other and state if the charge on each side-chain is positive or negative.

(3 marks)

(i)

(ii)

c) Choose an amino acid that could participate in a disulfide bond and name the

amino acid. (1 mark)

4. The figure below shows a region of a polypeptide chain.

a) Draw the resonance structure that leads to the partial double-bond character of

the peptide bond. (2 marks)

b) By describing the architecture of an alpha helix, explain why the resonance

structures, described in (a), lead to a helix having a net dipole moment.

(3 marks)

5. The diagram below shows an amino acid with a post-translational modification

(not all the atoms and bonds are shown).

a) Name the specific type of modification. (2 marks)

b) Provide the amino acid sequence context (sequence of three amino acids with

the first one being modified) in which it occurs. (2 marks)

___________________________________________________________

6. a) Draw two D-aldose pentose sugars in Fischer projection that are epimers.

(4 marks)

b) Circle the carbon centres whose stereochemistry is used to assign the chirality

of each aldose sugar molecule. (1 mark)

7. Draw docosahexaenoic acid (C22:6Δ4,7,10,13,16,19). (3 marks)

8. Where is a secreted protein synthesised? Describe the sequence of events that

must occur in order for such a protein to reach its destination. (4 marks)

9. a) Draw a sketch graph to illustrate the relationship between substrate

concentration and rate of an enzyme-catalysed reaction, showing the

approximate values of the key enzymological parameters Vmax and KM. (4 marks)

b) What happens to Vmax and KM in the presence of a non-competitive inhibitor?

(2 marks)

c) Illustrate how a non-competitive inhibitor interacts with an enzyme, and how

this is different from the interaction between a competitive inhibitor and the

enzyme. (3 marks)

10. a) State four features of a typical enzyme active site. (4 marks)

(i)

(ii)

(iii)

(iv)

b) The enzyme carbonic anhydrase catalyses the reversible interconversions of

carbon dioxide and water to carbonic acid (H2CO3). How does the active site

allow this reaction to be catalysed? (4 marks)

c) The conversion of carbon dioxide to carbonic acid occurs spontaneously at a

low rate. Why is it necessary for humans to have an enzyme to carry out this

process? (1 mark)

11. a) In the table below, rank the fuels glucose, fatty acids and glycogen for energy

density and preference. (3 marks)

Generating most (i) to least (iii)

amount of ATP per gram of fuel

Most (i) to least (iii) preferred by the

human body as an energy source

i)

ii)

iii)

b) The two rank orders do not agree. Why? (4 marks)

___________________________________________________________

12. a) Why is fermentation essential for mammals in the absence of oxygen?

(3 marks)

b) What is the role of the urea cycle? (2 marks)

c) Why is fructose-1,6-bisphosphate cut in half by aldolase? (2 marks)

___________________________________________________________

13. During extreme starvation when glycogen reserves have been fully depleted,

assume that the body’s energy needs are satisfied purely by the catabolism of

palmitate released from adipose tissue.

a) Given that the brain could consume up to 40% of the resting energy needs of

the body during extreme starvation, what percentage of the palmitate enters the

TCA cycle in non-brain tissues? (5 marks)

b) What percentage of the total CO2 is released by the brain? (1 mark)

Fun with enzymes

This just shows some important words in the topic Enzymes.

Reference:
Tagxedo. http: http://www.tagxedo.com/. Accessed 12th April,2013.

For ice- cream lovers, take just 2:54 out of your busy UWI life and watch this talking ice- cream. You’ll enjoy it !

This video just gives health information on a highly consumed treat by all ages.

Reference:
Eat Healthly, Kids! Funny Cartoon. 2009. http://www.youtube.com/watch?v=arKj1xgWHZo. Accessed 11th April, 2013.