Option B - Human biochemistry Flashcards
(130 cards)
Outline how respiration makes energy out of glucose

How is a bomb calorimeter used to measure the energy value of food samples?
- The food is burned to completion in the bomb
- The heat released as it burns is measured by the temperature rise in a known mass of pure water
- The specific heat capacity of the water is used to calculate how much energy was used to increase the temperature with the following formula:
Q = cm∆T

Draw the general formula of 2-amino acids

What defines an amino acid?
Its R group
What is a buffer?
A solution which resists changes in pH on the addition of a small amount of acid or alkali
What are the three major chemical properties of amino acids?
- Form zwitterions
- Work as buffers
- Have isoelectric points
Describe how amino acids form zwitterions
- Internal acid-base reaction
- The acidic –COOH transfers a proton to the basic –NH2 group in the same amino acid

Describe the ionic properties of amino acids
- Crystalline compounds
- High melting points, usually over 200°C
- Much greater solubility in water than in non-polar solvents
- Move in an electric field
Describe the amphoteric properties of amino acids
- Contain both an acid and a basic group
- Are able to react with both bases and acids
- In zwitterion form

Why is the buffering nature of amino acids important?
- Due to the zwitterion ion and amphoteric nature of amino acids
- Help in maintain constancy of the pH in body cells
- Proteins are extremely sensitive to change in pH
What is meant by the isoelectric point of an amino acid and what are its properties?
An intermediate at which the amino acid is electrically neutral
- Amino acids won’t move in an electric field
- The molecules have minimum mutual repulsion → least soluble
- Different amino acids have different isoelectric points
- If the R group contains an acidic or a basic compound, the pKa and pKb of these groups will affect the charge as pH changes
What is the relationship between pH and the charge on amino acids?
- pH determines the net charge that the amino acid carries
- Positively charged at low pH
- Negatively charged at high pH

How are amino acids condensed together?
- Condensation rection in which a molecule of water is eliminatend and a new bond is formed between the acids
- Called a peptide bond
- Two acids are a dipeptide, three acids a tripeptide, and eventually a polypeptide is formed
- The acid group (—COOH) of one acid and the amino group (—NH2) of the other join together
- After the condensation there are free functional groups on both ends to the peptide can undergo further condensation

What is the primary structure of a protein?
The number and sequence of amino acids in its polypeptide chain
(e. g. Asn-Cys-Val-…)
- The covalent backbone of the molecule
- Dictates the entire structure and function of the protein
- The alteration of just one amino acid can completely change the function of the protein
What is the secondary structure of proteins?
- Either α-helix or β-pleated sheet
- Folding of the polypeptide chain as a result of hydrogen bonding
- Bonds can form between the –C=O group of one peptide and the –N–H group of another
What is the α-helix secondary structure of proteins?
- Regular coiled configuration of the polypeptide chain
- Hygrogen bonds between two peptide bonds four amino acid units apart
- This twists the chain into a tightly coiled helix (spiral staircase)
- Flexible and elastic because the intra-chain hydrogen bonds easily break and reform when stretched
- E.g. keratins = structural proteins in hair, skin, and nails

What is the β-pleated sheet secondary structure of proteins?
- Side by side polypeptides bonded together
- Not tightly coiled
- Arranged in pleated sheets that are cross-linked by inter-chain hydrogen bonds
- Flexible but inelastic
- Found in webs of spiders and silkworms and the beaks and claws of birds

What is the tertiary structure of proteins?
- Further twisting, folding, and coiling of the polypeptide chain
- A result of interactions between the R groups (side chains)
- Very specific compact three-dimensional structure (conformation)
- The most stable arrangement of the protein
- Takes into account all the possible interaction between the side chains
- Intra-molecular forces as they occur within one chain
What is meant by an enzyme’s conformation?
Its very specific compact three-dimensional structure.
Why is the tertiary structure of proteins important?
- Important in globular proteins (enzymes and proteins)
- Water soluble
- Specific structure necessary for the enzymes
What kind of interactions define and maintain the conformation of a protein?
- Hydrophobic interactions
- between non-polar side chains (e.g. van der Waals’) - Hydrogen bonding
- between polar side chains - Ionic bonding
- between side chains carrying a charge - Disulfide bridges
- between the sulfur atoms
- covalent bonds and the strongest of the interactions

What is the quaternary structure of a protein?
- The association between different polypeptides
- E.g. collagen: a triple helix of three polypeptide chains, with inter-chain hydrogen bonds in between → stable rope-like structure that is resistant to stretching
- E.g. haemoglobin: four polypeptide chains, two α and two β, bound together tightly around an iron

What needs to be done to proteins before they can be analysed?
They need to be split into their amino acids. The peptide bonds are broken through hydrolysis (reverse condensation)
What are the two ways of analysing proteins?
- Chromatography
- Electrophoresis





































