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HUMANBIOCHEMISTRY    -fatin    -hanis    -bella
B1.1: CALCULATE THE ENERGY VALUE OF A  FOOD FROM ENTHALPHY OF COMBUSTION                   DATA             ∆H = mc∆TKeys:...
Example:1.00 g cereal raises the temperature of 400 cm3water in an insulated food calorimeter from23.7 C° to 33.4 C°. Calc...
B2.1: DRAW THE GENERAL FORMULA OF             2-AMINO ACIDS• Central carbon of amino acids is made up of  hydrogen (H), am...
B2.2: DESCRIBE THE CHARACTERISTIC       PROPERTIES OF 2-AMINO ACIDS• Amino acids are:  – Colorless  – Crystalline solids  ...
H2NCHRCOOH + H2O               H3N+CHRCOOH + OH-At lower pH, H+ added reacts with OH- and theforward reaction is favoured ...
H2NCHRCOOH + H2O              H2NCHRCOO- + H3O+  At higher pH, the base added react with H3O+and the forward reaction is f...
When a strong acid is added to an aqueous solution of amino acid, the zwitterions accepts the proton thusminimizing the ef...
If a strong base is added, the zwitteriondonates H+ to neutralize the base to form                   water.
B 2.3 : DESCRIBE THE CONDENSATION           REACTION OF2 - AMINO ACID TO FORM POLYPEPTIDES
Amino acid contain both an amine functional group and acarboxylic acid function group.When they are both attached to the s...
There are about twenty 2-amino acid thatoccur naturally.All the twenty 2-amino acid are the basic“building block” of prote...
This process call as condensation reaction as it involve the formation ofwater molecule.The reaction between two amino aci...
The process of condensation polymerization is repeated untillong chain of amino acids is formed that is known aspolypeptid...
One example of alanine and glycine, can form two  dipeptides:NOTE: Alanine : have CH₃ on carbon molecule. Glycine : just...
B 2.4 : DESCRIBE ANDEXPLAIN THE STRUCTURE      OF PROTEIN
PRIMARY STRUCTURE : Definition : Linear sequences of amino acids in  polypeptides chain. Primary structure of protein is...
SECONDARY STRUCTURE :  Secondary structure is the chain of amino acid that  folds itself due to the intramolecular hydroge...
TERTIARY STRUCTURE : Tertiary structure is the overall folding of chain by interaction between  distant amino acid and gi...
QUARTERNARY STRUCTURE :Quaternary structure : separatepolypeptides chains can interact together to give amore complex stru...
B 2.5 Explain how proteins can be analyzed by           chromatography and electrophoresis.                               ...
Rf value =           =             x   y
Alternative ways :If sample of known amino acid is not available, Rfvalue (retention factor) can be measured andcompared w...
Electrophoresis• Structure of amino acid changes at different value of  pH.• At low pH (acidic medium), amine group will b...
Procedures :• Electrophoresis is carried out in polyacrylamide gel as  medium. Hence, the process is called PAGE (polyacry...
B2.6 List the major functions of proteins                     in the body.1.   Structural•    Protein such as collagen (fo...
B1 & b2  energy + protein
B1 & b2  energy + protein
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B1 & b2 energy + protein

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B1 & b2 energy + protein

  1. 1. HUMANBIOCHEMISTRY -fatin -hanis -bella
  2. 2. B1.1: CALCULATE THE ENERGY VALUE OF A FOOD FROM ENTHALPHY OF COMBUSTION DATA ∆H = mc∆TKeys:m = massc = specific heat of water (4.18 Jg-1C°-1)∆T = change in temperature
  3. 3. Example:1.00 g cereal raises the temperature of 400 cm3water in an insulated food calorimeter from23.7 C° to 33.4 C°. Calculate the energy valueper gram of the cereal, assuming the heatcapacity of the calorimeter is negligible andgiven the specific heat of water = 4.18 Jg-1C°-1(answer: 16.2 kJ per gram of cereal)
  4. 4. B2.1: DRAW THE GENERAL FORMULA OF 2-AMINO ACIDS• Central carbon of amino acids is made up of hydrogen (H), amino group (-NH), carboxylic acid group (-COOH) and side chain (R)
  5. 5. B2.2: DESCRIBE THE CHARACTERISTIC PROPERTIES OF 2-AMINO ACIDS• Amino acids are: – Colorless – Crystalline solids – Exist as zwitterions (dipolar ions) – Relatively high melting points – More soluble in water than organic solvents – Are amphoterics (capable of behaving as acids or bases)
  6. 6. H2NCHRCOOH + H2O H3N+CHRCOOH + OH-At lower pH, H+ added reacts with OH- and theforward reaction is favoured to replace some ofthe OH- used up. Thus, in an acidic solution, the-NH2 group is protonated.
  7. 7. H2NCHRCOOH + H2O H2NCHRCOO- + H3O+ At higher pH, the base added react with H3O+and the forward reaction is favoured to replacesome of the H3O+ used up. Thus, in an alkalinesolution, the carboxylic acid group donates aproton and converted to the carboxylate ion.
  8. 8. When a strong acid is added to an aqueous solution of amino acid, the zwitterions accepts the proton thusminimizing the effect of the acid added.
  9. 9. If a strong base is added, the zwitteriondonates H+ to neutralize the base to form water.
  10. 10. B 2.3 : DESCRIBE THE CONDENSATION REACTION OF2 - AMINO ACID TO FORM POLYPEPTIDES
  11. 11. Amino acid contain both an amine functional group and acarboxylic acid function group.When they are both attached to the same carbon atom, theyknown as 2-amino acid or α–amino aciddiagram of 2-amino acid or α–amino acid : H H₂N C COOH R -2-amino acid-
  12. 12. There are about twenty 2-amino acid thatoccur naturally.All the twenty 2-amino acid are the basic“building block” of protein in our body.It consist of long polypeptides whichformed by condensation reactionbetween amino acid.All amino acid have both a carboxyl groupand an amino group which they able toundergo condensation reaction to formsubstituted amides.
  13. 13. This process call as condensation reaction as it involve the formation ofwater molecule.The reaction between two amino acid result in the formation of adipeptide and water.Definition of dipeptide : a product which is a substituted amide made upof two amino acid joined by a peptide bond or peptide linkage.The two amino acid residues are joined by a strong carbon - nitrogenbond.
  14. 14. The process of condensation polymerization is repeated untillong chain of amino acids is formed that is known aspolypeptides.
  15. 15. One example of alanine and glycine, can form two dipeptides:NOTE: Alanine : have CH₃ on carbon molecule. Glycine : just have H on the carbon molecule.
  16. 16. B 2.4 : DESCRIBE ANDEXPLAIN THE STRUCTURE OF PROTEIN
  17. 17. PRIMARY STRUCTURE : Definition : Linear sequences of amino acids in polypeptides chain. Primary structure of protein is determined by the sequence of bases in gene that codes for protein. If there is changing if a single amino acid due to a mutation in DNA of its gene will alter its properties drastically. Example: sickle anaemia cell. Each protein has its own unique primary sequence if amino acid. Primary structure of protein gives the protein ability to carry out its characteristic function. Eg : a tripeptide containing the amino acid : lysine, glycine and leucine lys-gly-leu
  18. 18. SECONDARY STRUCTURE : Secondary structure is the chain of amino acid that folds itself due to the intramolecular hydrogen bond. Two type of secondary structure : α-helix : the protein is twist in a spiralling manner like coiled spring. β pleated sheet : give a sheet- like structure. Example of : α-helix : keratin that found in nail and hair β pleated sheet : silk fibre
  19. 19. TERTIARY STRUCTURE : Tertiary structure is the overall folding of chain by interaction between distant amino acid and gives protein its three-dimensional shape of single protein. (when the secondary structure is folded further to form 3D shape of globule) Tertiary sturucture of protein is folded each other because of they have attraction between amino acid in polypetides The interaction that involve : Hydrogen bond Van Der Waal’s between non polar side group Ionic attraction between polar groups Disulphide bridge Example of tertiary structure of protein : Immunoglobin Antibody Enzyme Insulin (Protein based hormone)
  20. 20. QUARTERNARY STRUCTURE :Quaternary structure : separatepolypeptides chains can interact together to give amore complex structure.Eg : Haemoglobin has quaternary structure that include 4 protein chain ( two α– chains and two β - chains) which is grouped together around four haem groups
  21. 21. B 2.5 Explain how proteins can be analyzed by chromatography and electrophoresis. Chromatography.•Primary structure of protein can be identified by chromatography paper orelectrophoresis.•However, protein must be hydrolyzed first by hydrochloric acid to successivelyrelease amino acids. Procedure :1. A small spot of an unknown amino acid sample is placed in a solvent (eluent) placed in developing tank with cover.2. Eluent rises up the paper due to capillary action.3. When it meets the sample spot, the different amino acid partition themselves between the eluent and the paper to some extents4. The move up at different rates.5. When the eluent almost reach the top, the paper is removed from the tank, dried up, and sprayed with organic dyes (ninhydrin) to develop chromatogram by coloring acids.6. Compare the position of all spots.
  22. 22. Rf value = = x y
  23. 23. Alternative ways :If sample of known amino acid is not available, Rfvalue (retention factor) can be measured andcompared with known values as each amino acidhad a different Rf value.Sometimes, we may found that two acids have thesame Rf value using the same solvent, but using adifferent solvent may result different Rf value.Chromatogram can be turned through 90o and runagain using the second solvent.
  24. 24. Electrophoresis• Structure of amino acid changes at different value of pH.• At low pH (acidic medium), amine group will be protonated.• At high pH (alkaline medium), the carboxylic group will lose a proton.• This is why amino cid can act as buffers.• If H is added, they are removed as –NH and if OH is added, -COOH will lose a proton to remove OH- ions in water.• For each amino acid, there is a unique pH value named isoelectric point where the acid exists as zwitterions.
  25. 25. Procedures :• Electrophoresis is carried out in polyacrylamide gel as medium. Hence, the process is called PAGE (polyacrylamide gel electrophoresis)• The sample is placed in the centre of the gel and potential different is applied across it.• Depending on the pH of amino acid, the sample will move at different rates toward the negative and positive electrodes.• At isolelectric point, a particular amino acid will stop moving as its charge is balanced already.• When separation is completed, the acids can be sprayed with ninhydrin and identified by comparing distances they have travelled with standard samples or from comparison of their isoelectric point.
  26. 26. B2.6 List the major functions of proteins in the body.1. Structural• Protein such as collagen (found under the skin) and keratin (found in hair and nails) provide structure and strength.2. Biological catalysts• Enzymes act as biological catalyst that speed up the reaction in human body by providing alternate pathways for the reaction. It lowers the activation energy of the reaction.3. Hormones• Insulin is essential for human body.4. Antibodies• Types of protein produced result to presence of any foreign materials in human body. It provide immunity against the diseases. For example, immunoproteins.5. Transport• Haemoglobin in red blood cells carry oxygen from lungs to the cell. It also carries carbon dioxide from cells to lung to be excreted out.6. Energy.• Protein can also be a source of energy for human. Instead of carbohydrates and fats, protein can also be metabolized to provide energy under certain condition.

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