Proteins

MS GLASGOW
Proteins- gps of organic compounds
consisting of C, H, O,N & Sometimes S
The amino acid has a chiral
The monomer is an amino acid carbon
Peptide Bonding
Categories of Amino Acids
 What happens when amino acids reacts with water?
Answer:
Zwitterion formed (contains separate parts which are +vely & -
vely charged)
Reason:
Internal transfer of a hydrogen ion from the -COOH group to the
-NH2 group -> ion with both a -ve charge & a +ive charge
In acidic solutions:
 The -COO- part of the zwitterion picks up a hydrogen ion,
resulting in a +vely charged amino acid (Left)
In basic solutions:
The hydrogen ion is removed from the -NH3+group, resulting in a
–vely charged amino acid (right)
Conclusion:
The zwitterion acts as a pH buffer ( able to resist changes in the
pH of its surrounding)
 Hydrogen Bonds

• Formed between R groups

w/h are dipoles e.g
carboxyl, hydroxyl &
amino groups

• Relatively weak bonds

 Ionic Bonds

• Formed between groups

with opposite charge e.g
ionised carboxyl and
amino groups

• Bond is stronger than H-

bonds
Disulphide Bonds

• Formed between R groups

contain S - atoms e.g
cysteine

• Strong covalent bonds due

to oxidation of 2 S – atoms
by dehydrogenation
Hydrophobic Interactions

• Formed with non-polar R

groups e.g. tyrosine &
valine

• In aq. Sol’n ->

hydrophobic group
gathers in the interior
away from water while
hydrophilic group forms
an outer shield towards
the water
Compare the different levels of protein
structure
OBJ 1.9
Protein Structure
Primary structure of
proteins
• Refers to the no. and
sequence of aa in the
polypetide chain
• Shape = Straight chain, i.e,
no folding
• Bond = peptide bond
• Its sequence is influenced
by the gene code to give a
particular protein /
phenotype
 Secondary structure of
proteins
• Refers to the shape of the polypeptide chain due to
H-bonding in the backbone of the aa in the same
polypeptide or between different polypeptides
• The shapes are either :
• alpha helix = H-bonds formed between double
bonded O of one aa and the H of the amino gp in
another aa w/h is 4 aa apart
• beta pleated sheets= H-bond formed between
doubled O/ amino gp in one aa of one chain with
doubled O / amino gp of another aa in another
chain/ another distant part of the chain to give a
zigzag pattern
• Bond = peptide and H-bonds
• NB Pr with these shapes as their final
configuration are known as fibrous Pr
 Tertiary structure of
proteins
• Refers to the shape of the polypeptide
chain due to bonds formed among R
groups of different aa in the polypeptide
chain
• The shape is 3D due to folding of the
chain & variable producing globular
proteins
• Bonds = peptide bonds, H-bonds as well
as 1 or more of the following: ionic,
disulphide, hydrophobic interactions
 Quaternary Structure of
proteins
• Refers to the shape of 2 or
more polypeptides bonding
together
• The shape is variable and the
structure may contain a
prosthetic group (non- pr g
required for proper
functioning)
• Bonds include peptide bonds,
H-bonds as well as 1 or more
of the following: ionic,
disulphide, hydrophobic
interactions
Outline the molecular structure o
haemoglobin as an example of a
globular protein and collagen as an
example of a fibrous protein
OBJ 1.11
Comparison of globular and fibrous
proteins
Fibrous
 Polypeptide chains are parallel with little or no
tertiary folding
 Different pr have similar shapes (helices) but
primary structure is variable
 Insoluble in water b/c polar groups are involved
in H-bonds
 Stable & tough re: H-bonds
 Func’n is structural
 Eg. Silk, collagen, keratin
Globular
 Polypeptide chains are folded into a tertiary
structure w/j is spherical & compact
 Pr have a specific shape
 Soluble in water making a colloidal sol’n re:
hydrophobics parts inward w/h cannot be dissolved
 Less chemically stable re: R gps bonds are easily
broken by change in env’t
 Func’n is metabolic
 Eg all enz, antibodies, haemoglobin
• Carries O2 in RBC
• Consists of 4 separate polypeptides Haemoglobin (Globular Protein)
• 2 alpha (141 aa) & 2 beta chains (146 aa)
• Each alpha & beta chain has helix and non-helix
segments
• The helix segments=> hydrophobic crevice where
Fe2+ binds
• NB H2O oxidises Fe2t to Fe3+ w/h cannot bind O2
• 1 haem gp in the hydrophobic centre of each
polypeptide w/h forms a temporary bond with 1 O2
• The O2 binds cooperatively, ie, binding of the 1st
makes it easier for the others to bind as the shape
changes from being tense to more relaxed
• Soluble in water re: hydrophobic side gp inward but
hydrophilic side gp outward towards water
• Sickle cell anaemia <- mutation <- hydrophilic R
group is replaced by a hydrophobic R group
• Extracellular pr
• Component of connective tissues such as Collagen (Fibrous Protein)
tendons & blood vessels & binds inorganic
crystals=> tensile strength & support
• Consists of 3 polypeptide chains with a left
hand helix orientation producing a triple
helix
• 3 helices linked by a right hand coil
stabilised by H-bonds
• Each chain of repetitions of 3 aa (proline,
glycine, alanine)
• The H of gly are on the inside while the R
groups of pro & ala are on the outside
• Insoluble in water re: long (1000 aa) &
hydrophobic R gps
• Assemble into flexible fibres w/h cannot
stretch
Food test
Reducing Sugars
Non-reducing Sugars
Starch
Protein
Lipids