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Protien AS

Proteins have a variety of important functions in living organisms. They are made up of amino acids that join together to form polypeptide chains that fold into complex shapes determined by interactions between their R groups. This folding leads to four levels of protein structure - primary, secondary, tertiary, and sometimes quaternary - that are essential to a protein's function. Globular proteins in particular adopt spherical shapes and perform metabolic roles like enzymatic reactions. Their precise tertiary structures form active sites that carry out functions but can become denatured and nonfunctional if their shapes change due to environmental factors like heat or pH.

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255 views25 pages

Protien AS

Proteins have a variety of important functions in living organisms. They are made up of amino acids that join together to form polypeptide chains that fold into complex shapes determined by interactions between their R groups. This folding leads to four levels of protein structure - primary, secondary, tertiary, and sometimes quaternary - that are essential to a protein's function. Globular proteins in particular adopt spherical shapes and perform metabolic roles like enzymatic reactions. Their precise tertiary structures form active sites that carry out functions but can become denatured and nonfunctional if their shapes change due to environmental factors like heat or pH.

Uploaded by

Rabia Rafique
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Proteins

Function of proteins.

• Proteins are very important in living organisms and


take on a variety of forms and functions:
• Enzymes.
• Antibodies.
• Actin and myosin
• Oxygen transport
• Keratin
• Hormones
• Membrane formation
The structure of proteins.
• Proteins are made up of carbon, hydrogen,
oxygen and nitrogen. Sometimes sulphur is
present.
• Proteins are polymers made up of the
monomers called amino acids.
• There are 20 different amino acids.
• Amino acids can join up in any order and form
an infinite number of protein molecules.
Amino acids.
• Amino acids contain an amino group (-NH2)
and a carboxylic acid group (-COOH).
• Each amino acid has an R group.
• There are 20 different R groups and this is the
reason for there being 20 different types of
amino acids.
Structure of an amino acid.
R Group

Amino Carboxylic acid


group group
How do two amino acids join together ?

• Two amino acids join together by


condensation to form a dipeptide .

A peptide
bond is
formed and
this results in
a dipeptide
What is a polypeptide?
• A chain of amino acids is known as a
polypeptide.
Proteins can be divided into groups.
• Globular proteins. These are molecules that
are often spherical in shape and have a
chemical function eg enzymes.
• Fibrous proteins . These have a structural
role . They give strength or elasticity to a
particular tissue eg keratin in hair.
Four levels of structure.
• Primary structure. A sequence of amino acids
in a polypeptide chain.
• Secondary structure. The chain of amino acids
bend and twist and forms a stable structure
that is held in position by hydrogen bonds. A
helix is the most common secondary
structure.
2- Secondary structure:
Results from hydrogen bond
formation between hydrogen of –NH
group of peptide bond and the carbonyl
oxygen of another peptide bond.
According to H-bonding there are two
main forms of secondary structure:
α-helix: It is a spiral structure resulting
from hydrogen bonding between one
peptide bond and the fourth one
β-sheets: is another form of secondary
structure in which two or more
polypeptides (or segments of the same
peptide chain) are linked together by
hydrogen bond between H- of NH- of one
chain and carbonyl oxygen of adjacent
chain (or segment).
• Tertiary structure. The secondary structure folds
to give a more three dimensional shape. The
shape is maintain by hydrogen bonds and the
stronger disulphide bridges which form between
the sulphur containing amino acids molecules.
• Such proteins are often called globular proteins.
their shape is vital to their function. Eg enzymes.
• Tertiary structure
is determined by a variety of
interactions (bond formation) among R
groups and between R groups and the
polypeptide backbone.
a. The weak interactions include:
 Hydrogen bonds among polar side
chains
 Ionic bonds between
charged R groups ( basic
and acidic amino acids)
 Hydrophobic
interactions among
hydrophobic ( non polar) R
groups.
b. Strong covalent bonds include disulfide bridges,
that form between the sulfhydryl groups (SH) of
cysteine monomers, stabilize the structure.
• Quaternary structure:results from the aggregation (combination) of two or
more polypeptide subunits held together by non-covalent interaction like H-
bonds, ionic or hydrophobic interactions.
• Examples on protein having quaternary structure:
– Collagen is a fibrous protein of three polypeptides that are supercoiled like
a rope.
•This provides the structural strength for their role in connective tissue.
– Hemoglobin is a globular protein with four polypeptide chains
– Insulin : two polypeptide chains
Globular proteins.
• Globular proteins have the following characteristics:
• Irregular amino acid sequence
• Sequence is highly specific and never varies between
2 examples of the same protein.
• Polypeptides fold into a spherical shape.
• Relatively unstable structure.
• Metabolic functions.
• Enzymes, hormones and haemoglobin.
Structure and function of globular
proteins.
• The shape of a globular protein is very delicate and
vital to it’s function.
• An enzyme has a precise tertiary structure that
provides it with it’s active site. Any change in the
shape of the active site will stop the enzyme from
working.
• High temperatures make the molecules vibrate and
this causes the weak hydrogen bonds to break and as
a result the shape changes. The enzyme is denatured
and will not work.
Denaturation of proteins.
• The three dimensional shape of proteins is
maintained by hydrogen bonds and ionic
bonds which are fairly weak.
• Any agent such as heat, acids or alkalis will
break these bonds and cause a change in
shape.
• With a change in shape the protein can no
longer carry out it’s function.
Questions.
1 Describe the general structure of an amino
acid.
2 With the aid of a diagram , show the results
when two amino acids are joined together.
3 Proteins may be described as having:
4 Primary, secondary, tertiary or quaternary
structures. Explain the meanings of these
terms when applied to proteins.
5 Describe the characteristics of a globular
protein.
6 How is the structure of a globular protein
related to it’s function?

7 What is meant by the term denatured?


8 Explain how a protein may become denatured.

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