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Lecture 5

Proteins have diverse functions and are one of the most abundant organic molecules. They can be structural, regulatory, catalytic, or protective. Enzymes are complex proteins that catalyze biochemical reactions like digestion. Each enzyme specifically binds to its substrate to break down, rearrange, or synthesize molecules. Amino acids are the building blocks of proteins and contain an amino group, carboxyl group, and unique R group. Peptide bonds link amino acids into polypeptide chains or proteins. Protein structure is hierarchical, from primary to quaternary levels. Changes in conditions can cause proteins to lose their shape through denaturation.

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11 views

Lecture 5

Proteins have diverse functions and are one of the most abundant organic molecules. They can be structural, regulatory, catalytic, or protective. Enzymes are complex proteins that catalyze biochemical reactions like digestion. Each enzyme specifically binds to its substrate to break down, rearrange, or synthesize molecules. Amino acids are the building blocks of proteins and contain an amino group, carboxyl group, and unique R group. Peptide bonds link amino acids into polypeptide chains or proteins. Protein structure is hierarchical, from primary to quaternary levels. Changes in conditions can cause proteins to lose their shape through denaturation.

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PROTEINS

Hamza Abu Hilail


M.Sc. Physiology
Proteins
• Proteins are one of the most abundant organic molecules in
living systems and have the most diverse range of functions of
all macromolecules.

• Proteins may be structural, regulatory, contractile, or


protective.

• They may serve in transport, storage, or membranes; or they


may be enzymes.
Types and Functions of Proteins
• Enzymes catalysts in biochemical reactions (like digestion) and are
usually complex proteins.

• Each enzyme is specific for the substrate (a reactant that binds to an


enzyme) upon which it acts.

• The enzyme may help in breakdown, rearrangement, or synthesis


reactions.

• The enzymes that break down their substrates called catabolic enzymes.
Types and Functions of Proteins
• The enzyme that build more complex molecules from their substrates
are anabolic enzymes

• enzymes that affect the rate of reaction are catalytic enzymes.

• all enzymes increase the reaction rate and, therefore, are organic
catalysts.

• An example of an enzyme is salivary amylase, which hydrolyzes its


substrate amylose, a component of starch.
Hormones
• Hormones are chemical-signaling molecules, usually small
proteins or steroids, secreted by endocrine cells that act to
control or regulate specific physiological processes, including
growth, development, metabolism, and reproduction.

• For example, insulin is a protein hormone that helps regulate


the blood glucose level.
primary types and functions of proteins
Proteins
• Proteins have different shapes and molecular
weights.

• Some proteins are globular in shape; whereas,


others are fibrous in nature.
 hemoglobin is a globular protein
 Collagen is a fibrous protein

• Protein shape is critical to its function

• Changes in temperature, pH, and exposure to


chemicals may lead to permanent changes in the
protein's shape, leading to loss of function, or
denaturation.
Amino Acids
• Amino acids are the monomers that comprise proteins.

• Each amino acid has the same fundamental structure, which consists of:
1. a central carbon atom, or the alpha (α) carbon
2. amino group (NH ) 2

3. carboxyl group (COOH),


4. Hydrogen atom.

• Every amino acid also has another atom or group of atoms bonded to the
central atom known as the R group
Amino Acids
structure
Amino Acids
• The name "amino acid" because these acids contain both amino
group and carboxyl-acid-group in their basic structure.

• there are 20 common amino acids present in proteins.

• Nine of these are essential amino acids in humans because the


human body cannot produce them and we obtain them from our
diet.

• For each amino acid, the R group (or side chain) is different
Amino Acids
• The chemical nature of the side chain determines the amino acid's nature
(that is, whether it is acidic, basic, polar, or nonpolar).
For example:
 glycine has a hydrogen atom as the R group.
 valine, methionine, and alanine are nonpolar or hydrophobic in nature
 serine, threonine, and cysteine are polar and have hydrophilic side
chains.
 lysine and arginine have positively charged in side chains, and therefore
these amino acids are also basic amino acids.
 amino group in Proline has an R group forma ring-like structure
Amino Acids
• Essential amino acids refer to those necessary to build proteins in the
body, but not those that the body produces.

• Essential amino acids in humans include isoleucine, leucine, and cysteine

• A covalent bond, or peptide bond, attaches to each amino acid, which a


dehydration reaction forms.

• One amino acids carboxyl group(COOH) and the incoming amino acid's
amino group (NH2) combine, releasing a water molecule.
peptide bond

combine carboxyl group(COOH) & amino group (NH2)


Amino Acids
• polypeptide is a short chain of amino acids (typically 2 to 50) linked by
chemical bonds peptide bonds

• The term protein is used for a polypeptide or polypeptides that have


combined together.

• After protein synthesis (translation), most proteins are modified;


known as post-translational modifications.

• They may undergo cleavage, phosphorylation, or may require adding


other chemical groups.
levels of protein
structure
1. Primary Structure

Primary structure: The unique


sequence of amino acids for
particular polypeptide

• Amino terminal (N terminal)


• Carboxyl terminal (C terminal)
Secondary Structure
• secondary structure of the protein:
The local folding of the polypeptide in
some regions

• The most common are:


1. α-helix
2. β-pleated sheet

• Both structures are held in shape by


hydrogen bonds.
• The hydrogen bonds form between the
oxygen atom in the carbonyl group in one
amino acid and another amino acid.
Tertiary Structure
Tertiary structure: The polypeptide's unique three-dimensional structure

 The interactions among R groups create the protein's complex three-


dimensional tertiary structure.
Tertiary Structure
The nature of the R groups in
the amino acids involved:
1. forming the hydrogen bonds.
2. R groups with unlike charges
are attracted to each other
(ionic bonds).
3. hydrophobic interactions.
4. Interaction between cysteine
side chains forms disulfide
linkages in the presence of
oxygen
 disulfide linkages is the only
covalent bond that forms
during protein folding.
Quaternary Structure
Quaternary structure: the overall
3D structure of the protein
Denaturation and Protein Folding
• protein denaturation: the protein losing its shape without losing its
primary sequence resulting from changes in temperature, pH, or
exposure to chemicals.
Denaturation is often reversible.
Sometimes denaturation is irreversible, leading to loss of function.

• Protein folding is critical to its function


• the proteins themselves were responsible for the folding process.
• proteins receive assistance in the folding process from protein helpers,
or (chaperones) that associate with the target protein during the folding
process.

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