Protein Structure

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• In general, for a protein molecule to serve a
specific biological function, it must have a
closely defined overall shape.
• Chemists typically describe large proteins on
several levels:
1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure

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• The primary structure of a protein is established
by the number, kind, and sequence of amino
acid units composing the polypeptide chain or
chains making up the molecule.
• The primary structure determines the alignment
of side-chain characteristics, which, in turn,
determines the three-dimensional shape into
which the protein folds.
• In this sense, the amino acid sequence is of
primary importance in establishing protein
shape.

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Figure 29.2 Amino acid sequence of beef insulin
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Primary structure of proteins
-always the same regardless of where the
the protein is found in an organism
Insulin, the hormone that regulates blood- glucose levels, was the first
proteins for which primary structure was determined.

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• The secondary structure of proteins can be
characterized as a regular three-dimensional
structure held together by hydrogen bonding
between the oxygen of the C=O and the hydrogen of
the H-N groups in the polypeptide chains.
• The a-helical and b-pleated-sheet structures are
two examples of secondary structure.

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Secondary Structure of Proteins
1. The Alpha helix structure
- A single protein chain adopts a shape that resembles a coiled spring
(helix) with the coil configuration maintained by hydrogen bonds

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Secondary Structure of Proteins
2. The beta pleated sheet
- a structure in which two fully extended protein chain segments
in the same or different molecules are together by hydrogen bonds

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 ………
Hydrogen
bonds

Figure 29. 1 The a-helix secondary structure.

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• The tertiary structure of a protein refers to
the distinctive and characteristic
conformation, or shape, of a protein
molecule.
• This overall three-dimensional conformation is
held together by a variety of interactions
between amino acid side chains.
• These interactions include:
1. Hydrogen bonding
2. Ionic bonding
3. Disulfide bonding

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 Tertiary structure of
proteins
• Hydrogen bonds can occur between amino acids with polar R
groups
- OH, -NH2, - COOH, - CO-NH2
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• Ionic bonding, also called salt bridges, always involve
interaction between an acidic side chain and a basic side
chain
• Disulfide bonds, the strongest of the tertiary –structure
interaction.

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• A quaternary structure is found in some
complex proteins.
• These proteins are made of two or more
smaller protein subunits (polypeptide
chains).
• The quaternary structure refers to the shape
of the entire complex molecule and is
determined by the way in which the
subunits are held together by noncovalent
bonds – that is, hydrogen bonding, ionic
bonding, and so on.

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Quaternary Structure of Proteins
- the highest level of protein organization
- found only in multimeric proteins
- the subunits are together are held together mainly by hydrophobic
interactions amino acid R groups

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 Protein
Classification based
on Shape
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Fibrous Proteins
• The fibrous proteins contain a highly developed
secondary structure.
• These proteins tend to function in support roles.
• The most abundant protein in the animal kingdom,
collagen, is a fibrous protein with a unique
secondary structure.

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Figure 29.3 A fibrous protein.

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Figure 29.3
Fibrous
proteins.

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 Globular Proteins
• The globular proteins share a similar
compact shape.
• The roughly spherical structure allows
each globular protein its own complex
tertiary structure.
• Each unique structure is associated
with a particular function.

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 Globular Proteins

• Myoglobin – a binding protein

• Carboxypeptidase A – an enzyme
• Immunoglobulin G – a binding protein
• Hemoglobin – a binding protein

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Protein Classification based on
function
-the functional versatility stems from
1. Their ability to bind small molecules
strongly to themselves
2. Their ability to bind other proteins to form fiber like
structures
3.Their ability to bind to, and become integrated into cell
membranes

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Protein Classification based on
function
1. Catalytic proteins - enzymes
2. Defense proteins- immunoglobulins or antibodies
3. Transport proteins – hemoglobin
4. Messenger proteins- hormones
5. Structural proteins – collagen

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Protein Classification based on
function
6. Contractile proteins – actin and myosin
7. Storage proteins – ferritin, myoglobin
8. Regulatory proteins – molecules that bind to enzymes turning them
“on and off,” thus controlling enzymatic action.
9. Nutrient proteins- casein, ovalbumin

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 Loss of
Protein Structure

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• If a protein loses only its natural three-dimensional
conformation, the process is referred to as
denaturation.
• Denaturation involves the alteration or disruption
of the secondary, tertiary, or quaternary– but not
primary- structure of proteins.
• Because a protein’s function depends on its natural
conformation, biological activity is lost with
denaturation.

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Figure 29.11 Structural change when a protein molecule is denatured:
The relatively weak hydrogen, electrostatic, and disulfide bonds are
broken resulting in a change of structure and properties (….denotes the
noncovalent bonds that stabilize a proteins natural conformation) 26
• Loss of protein structure also
occurs with hydrolysis of the
peptide bonds to produce free
amino acids.
• This chemical reaction destroys
the protein’s primary sequence.

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Protein Denaturation

Coagulation – the precipitation out of biochemical solution of

denatured protein which results to loss of water solubility

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Protein Denaturation
- Cooking foods kills microorganisms through protein denaturation
- in surgery, small wounds can be sealed by cauterization
- Sterilizing surgical instruments
- Canning of foods

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Protein Denaturation

Patient with fever – enzymes may begin to be inactivated through

denaturation
-the effect of ultraviolet radiation from the sun
- Serious eye damage can result from eye tissue contact with acids and
bases
- Use of alcohol as a disinfectant

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Tests for Proteins
and Amino Acids

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 Tests for Proteins and Amino
Acids
• Many tests have been devised to detect and distinguish among amino
acids, peptides and proteins.
• Xanthoproteic Test
• Biuret Test
• Ninhydrin Test

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