HS BIO 001 - TIPSHS

– PROTEINS –
- Performs many vital functions in the body such as:
- Structural support; enzymes; movement; transport; recognition and
receptor molecules; regulation of proteins and DNA; hormones;
antibodies; toxins and venoms
- The monomer of proteins is called AMINO ACID.

AMINO ACID

- Organic compounds containing an amine and carboxylic group and a

carbon chain specific to an amino acid.

Amino acid general

structure

- Amino acids bond covalently to form peptides and polypeptides

- Peptide bonds happen between the terminal carboxyl of one amino acid
and terminal amino group of the next amino acid.
- A dehydration synthesis reaction occurs and forms the peptide bond.
-
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- Disulfide bond happens between two terminal sulfhydrils of different

amino acids

TYPES OF PROTEINS

1. Primary structure is the unique sequence of amino acids forming a

polypeptide
- Primary structure of a protein is the precise sequence in which amino
acids are linked
- Changing even a single amino acid alters secondary, tertiary, and
quaternary structures – which can alter or destroy the biological function
of a protein
- Example: Substitution of a single amino acid in hemoglobin produces an
altered form responsible for sickle-cell disease
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2. Secondary structure is produced by the twists and turns of the amino acid
chain

- The amino acid chain (primary structure) is folded into arrangements that
form the protein’s secondary structure
- Amino acid side groups extend outward from the twisted backbone

ARRANGEMENT OF SECONDARY STRUCTRES:

• The alpha (α) helix is twisted into a regular right-hand spiral
• The beta (β) strand/pleated sheet zigzags in a flat plane, forming a sheet

alpha (α) helix beta (β) strand/

pleated sheet

3. Tertiary structure is the folding of the amino acid chain, with its secondary
structures, into the overall 3Dshape of a protein
- Tertiary structure gives a protein its overall three-dimensional shape, or
conformation
- The positions of secondary structures, disulfide linkages, and hydrogen
bonds play major roles in folding each protein into its tertiary structure
- Attractions between positively and negatively charged side groups and
polar or nonpolar associations also contribute to tertiary structure
- Tertiary structure determines a protein’s function
- The distribution and 3-D arrangement of side groups, in combination with
their chemical properties, determine the overall chemical activity of the
protein
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- Tertiary structure also determines the solubility of a protein, depending on

the arrangement of polar (hydrophilic) and nonpolar (hydrophobic)
segments Tertiary structure of most proteins is flexible, allowing them to
undergo limited conformational changes
- Conformational changes are important to the function of enzymes, and
to proteins involved in cellular movements or transport of substances
across cell membranes

- DENATURATION - Unfolding a protein from its active conformation so that it

loses its structure and function (caused by chemicals, changes in pH, or
high temperatures)
- For some proteins, denaturation is permanent – for others, denaturation is
reversible (renaturation)
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4. Quaternary structure – when present, is formed from more than one

polypeptide chain
- Some complex proteins, such as hemoglobin and antibody molecules,
have quaternary structure the presence and arrangement of two or more
polypeptide chains
- Hydrogen bonds, polar and nonpolar attractions, and disulfide linkages
hold the multiple polypeptide chains together
- In many proteins, folding of the amino acid chain (or chains) produces
large subdivisions called domains
- In proteins with multiple functions, individual functions are often located in
different domains
- Domains with similar functions are found in different proteins
- 3-D arrangement of amino acid chains within and between domains
produces highly specialized regions called motifs