Protein And Lipid Flashcards
Mention the functions of proteins and examples
- Act as enzymes (pepsin, DNA polymerase)
- Structural proteins (Keratin, collagen)
- Act as carrier and transport (Haemoglobin, aquaporin)
- Require for cell signalling (insulin & other hormones )
- Involve in defense mechanism (antibodies)
- As storage (bean seed proteins)
What is the structure for proteins and what are the classes and number of amino acids
Made up of chain of amino acids that are joined together by peptide bonds. Peptides: fewer than 50 aa Dipeptides: 2 aa Tripeptides: 3 aa Polypeptides: more than 10 aa Protein: more than 50 aa
Describe the strcuture of amino acid
Amino acid consist of central carbon atom which is alpha carbon amino group carboxyl group and a R group
The R group is a variable group that is different for each amino acid that gives unique chemical properties to each amino acid.
How is a peptide bond formed between amino acid
During condensation reaction when a water molecule is removed, a covalent bond is formed between amine group of one amino group to a carboxyl group of another forming a C-N bond.
This bond is broken by hydrolysis
Difference between essential, nonessential and conditional amino acids
Essential: Must be consumed in the diet
Nonesential: Can be synthesized in the body
Conditionally essential: Cannot be synthesized due to illness or lack of necessary precursors
Give an example of conditionally essential amino acid
Arginine, premature infants lack sufficient enzymes required too create arginine.
Why are the amino acids nonpolar and hydrophobic?
Why are these amino acids polar and hydrophillic
What is the name of the bond between sulfur and amino acid
Disulfide bridges
Types of folding in secondary and tertiary protein structures.
Secondary: Local folding along short sections of polypeptide and interaction between adjacent amino acids.
Tertiary: Whole molecule folding interactions between distant amino acids
Types of bonds in different levels of structure
Primary: Peptide bond
Secondary: Hydrogen bonds (weak bonds), alpha-helix and beta-pleated sheets.
Tertiary: Hydrophobic interactions, van der Waals interactions, hydrogen bonds, ionic bonds, disulfide bridges, covalent bonds between sulfurs in sulfhydryls.
Quaternary structures:
Hydrophobic interactions
Conditions required for disrupting bonds of proteins (protein denaturation)
Heat Acid Bases Salts Mechanical agitation
What happens to the protein during protein denaturation
Unfavourable condition alter secondary and tertiary structure but does not change the primary strucutre. It alters 3D shape and destroys functionality.
Only some proteins can return to their functional shape.
Protein strcuture obtained by what methods
X-ray crystallography
NMR- Nuclear Magnetic Resonance
Is lipid a polymer like proteins, nucleic acids, polysaccharides?
NO