Professional Documents
Culture Documents
Carbohydrates Are The Most Abundant Organic Compounds in PLANT WORLD
Carbohydrates Are The Most Abundant Organic Compounds in PLANT WORLD
LIPIDS
1. LIPIDS are insoluble in water, but soluble in hexane, acetone and diethyl ether.
2. The three most abundant fatty acids are palmitic acid, stearic acid, and oleic acid.
3. Most UNSATURATED fatty acids have a CIS-configuration; trans are rare.
1. -AMINO ACIDS are those amino acids with its amino group adjacent to the carboxylic group. These amino
acids are the most important class.
2. ZWITTERION is an internal salt of an amino acid, which has no net charge.
3. SIPIDER SILK has the amino acids glycine (42%) and alanine (25%).
4. L-DESIGNATION does not mean that the amino acid will rotate the plane of polarized light in the (-)
direction but it imposes the similarity of an L-amino acid to the reference compound, L-glyceraldehyde.
Instead of this, R and S configuration is used.
5. ISOELECTRONIC POINT (pI) is the pH at which majority of the molecule in an aqueous solution has a net
charge of zero.
6. ELECTROPHORESIS is the process of separating compounds on the basis of their total charge and this is
used to separate mixtures of amino acids and proteins.
7. PEPTIDE BOND is the bond formed by linking of an -amino group of one amino acid to the -carboxyl
group of another amino acid.
8. N-TERMINAL AMINO ACID is the free NH3+ terminal and C-TERMINAL AMINO ACID is the free COO-
terminal of a series of amino acids linked by peptide bonds.
9. PRIMARY STRUCTURE (1) is the sequence of the amino acids in the polypeptide which indicates all the
covalent bonding, read from the N to the C-terminal amino acid.
10. FREDERICK SANGER determined the amino sequence of the hormone insulin.
11. TRYPSIN catalyzes the cleavage of arginine and lysine while CHYMOTRYPSIN catalyzes the cleavage of
phenylalanine, tyrosine, and tryptophan.
12. EDMAN DEGRADATION the repetitive and selective cleaving of N-terminal amino acid for the
determination of the amino acid sequence.
13. LINUS PAULING first studied the geometry of peptide bonds discovering that it is planar.
14. SECONDARY STRUCTURE (2) is the ordered arrangement (conformation) of amino acid in localized
region of polypeptide or protein molecule. This structure is either -helix or -pleated sheet.
15. -HELIX has its polypeptide chain coiling as a spiral, commonly right-handed. Each peptide bond is trans
planar with 3.6 amino acids per turn of helix. It is stabilized by the hydrogen bonding of N-H and C=O bond
within the same polypeptide chain.
16. -PLEATED SHEET has its polypeptide section in parallel or antiparallel with each other. It is stabilized by
hydrogen bonding of N-H and C=O of the adjacent chain.
17. TERTIARY STRUCTURE (3) refers to the overall folding pattern and arrangement in space of all atoms in
a single polypeptide chain. The most important factors are the disulfide bond, hydrophobic interaction,
hydrogen bonding and salt linkages.
18. MYOGLOBIN consists of a single polypeptide chain of 153 amino acids with a single heme unit of one Fe +2
ion. Its 3 structure was discovered by John Kendrew and Max Perutz who shared the Nobel Prize in
Chemistry in 1962.
19. QUATENARY STRUCTURE (4) is the arrangement of monomers into aggregation. Its major factor for
stabilization is the hydrophobic effect.
33.