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Proteins PDF

Proteins are polymers made of amino acid monomers. The sequence and types of amino acids determine a protein's shape and function. There are 20 common amino acids that differ in their side chains. Peptide bonds form between amino acids via condensation reactions, linking them into polypeptide chains. Proteins fold into complex structures including primary, secondary, tertiary, and sometimes quaternary levels defined by bonding patterns that influence a protein's role in the body.

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72 views7 pages

Proteins PDF

Proteins are polymers made of amino acid monomers. The sequence and types of amino acids determine a protein's shape and function. There are 20 common amino acids that differ in their side chains. Peptide bonds form between amino acids via condensation reactions, linking them into polypeptide chains. Proteins fold into complex structures including primary, secondary, tertiary, and sometimes quaternary levels defined by bonding patterns that influence a protein's role in the body.

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Ashley Arnold
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© © All Rights Reserved
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Amino Acids Structure

Proteins

• Proteins are polymers (and macromolecules) made of monomers called amino


acids
• The sequence, type and number of the amino acids within a protein determines
its shape and therefore its function
• Proteins are extremely important in cells because they form all of the following:
o Enzymes
o Cell membrane proteins (eg. carrier)
o Hormones
o Immunoproteins (eg. immunoglobulins)
o Transport proteins (eg. haemoglobin)
o Structural proteins (eg. keratin, collagen)
o Contractile proteins (eg. myosin)

Amino acids

• Amino acids are the monomers of polypeptides


• There are 20 amino acids found in proteins common to all living organisms
• The general structure of all amino acids is a central carbon atom bonded to:
o An amine (also called amino) group -NH2
o A carboxylic acid group -COOH
o A hydrogen atom
o An R group (which is how each amino acid differs and why amino acid
properties differ e.g. whether they are acidic or basic or whether they are
polar or non-polar)

The general structure of an amino acid


Polypeptides & Protein Structure
• Peptide bonds form between amino acids
• Peptide bonds are covalent bonds and so involve the sharing of electrons
• In order to form a peptide bond :
o A hydroxyl (-OH) is lost from the carboxylic group of one amino acid
o A hydrogen atom is lost from the amine group of another amino acid
• The remaining carbon atom (with the double-bonded oxygen) from the first amino
acid bonds to the nitrogen atom of the second amino acid
• This is a condensation reaction so water is released
• Dipeptides are formed by the condensation of two amino acids
• Polypeptides are formed by the condensation of many (3 or more) amino acids
• A protein may have only one polypeptide chain or it may have multiple chains
interacting with each other
• During hydrolysis reactions, the addition of water breaks the peptide
bonds resulting in polypeptides being broken down to amino acids

Peptide bonds are formed by condensation reactions (releasing a molecule of


water) and broken by hydrolysis reactions (adding a molecule of water)

Primary, Secondary & 3-D Structure of Proteins


• There are four levels of structure in proteins
o Three are related to a single polypeptide chain
o The fourth level relates to a protein that has two or more polypeptide
chains
• Polypeptide or protein molecules can have anywhere from 3 amino acids
(Glutathione) to more than 34,000 amino acids (Titin) bonded together in chains

Primary structure

• The sequence of amino acids bonded by covalent peptide bonds is the primary
structure of a protein
• The DNA of a cell determines the primary structure of a protein by instructing
the cell to add certain amino acids in specific quantities in a certain sequence.
This affects the shape and therefore the function of the protein
• The primary structure is specific for each protein (one alteration in the sequence
of amino acids can affect the function of the protein)

An example of the primary structure of proteins showing the three-letter


abbreviation of specific amino acids

Secondary structure

• The secondary structure of a protein occurs when the weak negatively charged
nitrogen and oxygen atoms interact with the weak positively charged hydrogen
atoms to form hydrogen bonds
• There are two shapes that can form within proteins due to the hydrogen bonds:
o α-helix
o β-pleated sheet
• The α-helix shape occurs when the hydrogen bonds form between
every fourth peptide bond (between the oxygen of the carboxyl group and the
hydrogen of the amine group)
• The β-pleated sheet shape forms when the protein folds so that two parts of
the polypeptide chain are parallel to each other enabling hydrogen bonds to
form between parallel peptide bonds
• Most fibrous proteins have secondary structures (e.g. collagen and keratin)
• The secondary structure only relates to hydrogen bonds forming between
the amino group and the carboxyl group (the ‘protein backbone’)
• The hydrogen bonds can be broken by high temperatures and pH changes
The secondary structure of a protein with the α-helix and β-pleated sheet shapes
highlighted. The magnified regions illustrate how the hydrogen bonds form
between the peptide bonds

Tertiary structure

• Further conformational change of the secondary structure leads to


additional bonds forming between the R groups (side chains)
• The additional bonds are:
o Hydrogen (these are between R groups)
o Disulphide (only occurs between cysteine amino acids)
o Ionic (occurs between charged R groups)
o Weak hydrophobic interactions (between non-polar R groups)
• This structure is common in 3D globular proteins
The 3D tertiary structure of proteins with hydrogen bonds, ionic bonds, disulphide
bonds and hydrophobic interactions formed between the R groups of the amino
acids

Quaternary structure

• Occurs in proteins that have more than one polypeptide chain working together
as a functional macromolecule, for example, haemoglobin
• The same bonds responsible for maintaining the tertiary structure of a protein will
also be involved in forming the quaternary structure
• Each polypeptide chain in the quaternary structure is referred to as a subunit of
the protein
The quaternary structure of a protein. This is an example of haemoglobin which
contains four subunits (polypeptide chains) working together to carry oxygen

Summary of Bonds in Proteins Table

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