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3) Proteins Summary 9744 2017
3) Proteins Summary 9744 2017
3) Proteins Summary 9744 2017
Proteins
Describe the structure of an amino acid and the formation and breakage of a peptide bond
Polypeptides
Amino acids are joined by a peptide bond via a condensation reaction with the removal of one water
molecule.
Further addition of amino acids results in the formation of a linear polymer called a polypeptide
o Regularly repeating part, the main chain, is referred to as the backbone.
o Variable part comprises the distinctive variable R groups
polypeptide folds into a specific three-dimensional shape / conformation
The nucleotide sequence in DNA determines amino acid sequence in polypeptide which determines types and locations of R groups which
determines R group interactions which determines 3D structure and function of protein.
Explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary structure of proteins, and describe
the types of bonding (hydrogen, ionic, disulfide and hydrophobic interactions) which hold the molecule in shape.
Prepared by: Mrs.S Nair & Mrs.Wong SH Raffles Institution (Yr 5-6) 1
The Cell & Molecules of Life (9744) Proteins 2017
Analyse the molecular structure of a protein with a quaternary structure e.g. haemoglobin as an example of a globular protein and collagen as
an example of a fibrous protein, and relate these structures to their functions.
Example Structure Function
Haemoglobin 1. Haemoglobin has a quaternary structure made up of 4 Fe2+ of haem group binds temporarily to O2, so 1 Hb
(globular protein) polypeptide subunits: 2 -globin subunits and 2 -globin molecule can carry up to 4 O2, at a time forming
transports subunits. Each subunit is made of globin polypeptide and a oxyhaemoglobin
oxygen in the prosthetic (non-protein) component called haem group. Each
blood haem group consists of a porphyrin ring and an iron ion
**(The binding of (Fe2+)
successive O2 molecules
facilitates binding of the 2. Each subunit is arranged so that most of its hydrophilic Thus haemoglobin is soluble in an aqueous
next. Binding of the 1st amino acid side chains are on external surface while its environment, can be transported and carry O2 from lungs
O2 molecule increases hydrophobic amino acid side chains are buried in interior to tissues vice versa
the affinity of
haemoglobin for oxygen
and hence facilitates the 3. The 4 subunits held together by intermolecular interactions As a result binding of one oxygen molecule to one
binding of the 2nd O2 formed between R groups (hydrogen bonds, ionic bonds and haemoglobin subunit induces a conformational change in
molelcule. Binding of the
2nd O2 molecule hydrophobic interactions). No disulfide bridges. remaining 3 subunits so that their affinity for oxygen
facilitates the binding of increases. This is known as the **cooperative binding of
the 3rd O2 molecule and oxygen.
so on.)
Collagen 1. A collagen molecule (aka tropocollagen molecule) consists
(fibrous protein) of three helical polypeptide chains (loose helices, not α-
an essential helices) wound around each other like a rope. (has quaternary
component of structure) Bulky and relatively inflexible proline and hydroxyproline
connective tissue 2. Each chain contains about 1000 amino acids and contain a residues confer rigidity on the molecule.
in the human repeating sequence, usually a repeating tripeptide unit:
body.. glycine-X-Y, where X is usually proline, Y is usually
hydroxyproline.
The tropocollagen molecule can form a compact
coil as almost every third amino acid in each
polypeptide chain is a glycine, the smallest
amino acid. This allows it to fit into the restricted
space in the center of the triple helix. Increases tensile strength (ability to resist snapping due
3. Extensive hydrogen bonds form between to stretching) and increases tensile strength and makes
residues of the polypeptides, hence interaction the molecule insoluble in water
with water molecules are limited.
4. Adjacent tropocollagen molecules are arranged in Staggered/overlapping arrangement minimizes points
a staggered manner of weaknesses along fibrils
5. Cross-linking (involving covalent bonds Greatly increases tensile strength.
involving lysine residues) of adjacent
tropocollagen molecules results in the formation of
fibrils.
6. Bundles of fibrils together form large and long Large size of collagen makes it insoluble, an important
collagen fibres. property for a structural molecule
Denaturation of proteins
3D shape of a protein may be changed by:
(a) Heat (affect hydrogen bonds, hydrophobic interactions)
(b) Acids/Alkalis (affect hydrogen and ionic bonds)
(c) Inorganic ions (affect ionic bonds)
(d) Organic solvents (affect hydrophobic interactions)
(e) Mechanical forces (affect hydrogen bonds)
NB: 1. Peptide bonds not affected. 2. Strength of bonds: hydrophobic interaction<H bonds<ionic bonds <disulphide bridges <peptide bonds
Prepared by: Mrs.S Nair & Mrs.Wong SH Raffles Institution (Yr 5-6) 2