Human Biochemistry Flashcards
Product of the condensation reaction of 2-amino acids to form polypeptides
dipeptide
a substituted amide made up of two amino acids joined by a peptide bond or a peptide linkage
Explain primary structure of proteins
Simply the sequence of amino acid residues that form the protein
Indicated by using three-letter codes for the amino acids
Explain the secondary structure of proteins
manner in which the polypeptide chain folds itself due to intramolecular hydrogen bonding
Affects arrangement in space of the polypeptide chain
alpha helix and beta pleated sheets
Explain alpha helix
Resembles a right handed spiral staircase or coiled spring
Can make the protein elastic or sponge-like in fibrous proteins such as hair and wool
Maintains its shape through regular intramolecular hydrogen bonds
hydrogen bond between negative polar side O of the carbonyl group (C=O) and the positive polar side of the -NH2 group of the third peptide bond down the chain
Explain beta-pleated sheet
Different polypeptide chains are bound together by hydrogen bonds to create an orderly alignment of protein chains in which the direction of H-bonding is perpendicular to the sheet structure giving rise to a repeating, pleated pattern.
Explain tertiary structure of proteins
Folding or curling due to the interaction between the sequence of amino acids that maintains the three dimensional shape of the protein.
Amino acid chains interact in 4 ways to stabilize their shapes
1) covalent bonding (disulfide bridges)
2) H-Bonding between NH2 and COOH
3) salt bridges (electrostatic attraction) between NH3 and COO- groups
4) R group side chain depending on its polarity
Explain Quaternary Structure
How the polypeptide subunits are held together in a precise, more complex 3-D structural arrangement
Occurs only in proteins that are composed of more than one polypeptide chain which are held together by non-covalent bonds
Consist of hydrophobic interactions, H-bonding and ionic bonds
What is a subunit?
When a protein consists of more than one polypeptide chain, each polypeptide chain is a subunit
What is denaturation?
When proteins lose their 3-D structure and hence biological activity
Why does denaturing affect the functioning of a protein
The exact shape is the key to the function of each of the numerous proteins in the body.
Most common cause of denaturing is heat, as in the case when an egg is fried or boiled
Explain analysis of proteins through chromatography
Used for analyzing separation of mixtures of substances which are otherwise not easily separated
Paper chromatography - relative solubility of different amino acids varies in the stationary phase (water, which is absorbed on the cellulose paper) and in the mobile phase (solvent)
Amino acids with greater solubility in the eluting solvent will travel further in the direction of the solvent flow
Ratio of fronts = distance travelled by compound/distance travelled by solvent
Electrophoresis
Method of separating molecules on the basis of their electric charges
In order to analyze a protein using electrophoresis, the peptide bonds in the protein must first by hydrolyzed to release the individual amino acids
List the major functions of proteins in the body
Proteins carry out many important functions in the body
Structural - collagen (skin) keratin (hair)
biological catalysts - enzymes
hormones - insulin
antibodies - proteins that are produced as a result of the presence of foreign materials in the body
transport - hemoglobin
energy - proteins in the human body can be used to provide energy
carbohydrates
Main energy source for our bodies and are vital to the synthesis of cells.
Serve as food sources for living organisms and provide the structural support for plants.
Most carbohydrates are changed to glucose through digestion
Cellulose is the major component of plant cells that cannot be digested by humans; it does provide fiber
Describe the structural features of monosaccharides
Smallest molecular units of carbohydrates with the general formula (CH2O)n where n=3 to 9
Aldehydes or ketones containing a carbonyl group and at least 2 hydroxyl groups
(glucose, galactose)