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Proteins

Isabel, Gabi, Vivien

Proteins Isabel, Gabi, Vivien
What is a protein? ● Almost everything done by living things depends on them! ●

What is a protein?

● Almost everything done by living things depends on them!

● Account for more than ½ dry mass of most living cells.

● Life depends on enzyme catalysts.

○ Chemical agents that speed up chemical reactions by lowering activation energy

● Most structurally sophisticated macromolecule of life

● Monomers= amino acids (there are 20) bonded with peptide bonds. Polymers= polypeptides.

● A protein is a functional molecule made of 1+ polypeptides folded and coiled into a unique 3D shape.

Protein Functions

1. Enzymatic Proteins: Accelerate chemical reactions; used in digestion.

2. Storage Proteins: Store amino acids; casein in milk is source of amino acids for babies.

3. Hormonal Proteins: Coordinate organism’s activities; insulin secreted from pancreas causes other tissues to take up glucose to regulate blood sugar.

4. Contractile/Motor Proteins: Movement; actin and myosin are responsible for muscle contraction.

blood sugar. 4. Contractile/Motor Proteins : Movement; actin and myosin are responsible for muscle contraction.

More Protein Functions

More Protein Functions 1. Structural Proteins : Support the body; collagen & elastin create fibrous connective

1. Structural Proteins: Support the body; collagen & elastin create fibrous connective tissues.
2. Receptor Proteins: Aid response of a cell to chemical stimuli; receptors on membranes of a nerve cell detect signals from other nerve cells.
3. Transport Proteins: Transport substances; hemoglobin transports oxygen.
4. Defensive Proteins: Antibodies inactivate/destroy viruses and bacteria.

substances; hemoglobin transports oxygen. 4. Defensive Proteins : Antibodies inactivate/destroy viruses and bacteria.

Monomers: Amino Acids

Monomers: Amino Acids ● Alpha carbon connected to an amino group, a carboxyl group, a hydrogen
● Alpha carbon connected to an amino group, a carboxyl group, a hydrogen atom, and
● Alpha carbon connected to an amino group, a
carboxyl group, a hydrogen atom, and R group
(Side Chain) that determines unique traits.
● Amino acids with nonpolar side chains (Leucine)
are hydrophobic and with polar side chains are
hydrophilic (Serine).
● Negative charge: acidic carboxyl group in
R-groups (aspartic acid).
● Positive charge: basic amino groups in R-groups
(lysine).
● Held together by peptide bonds formed through
a dehydration reaction; side chains extend from
polypeptide backbone.

Protein Structure is SUPER COMPLEX

A functional protein isn’t just

a polypeptide chain; it’s one

or more polypeptides specifically

twisted/folded/coiled into a unique shape.

Amino acid sequence determines shape.

A

protein’s shape

determines its function.

 

There are four levels of structure within a protein.

  There are four levels of structure within a protein. Wireframe Model: Shows the backbone with

Wireframe Model: Shows the backbone with the side chains extending from it.

Space Filling Model: Able to show globular (spherical) shape;

Ribbon Model:

Shows how a polypeptide chain folds and coils.

Primary Structure

Sequence of amino acids that make up the polypeptide chain.

● The precise primary structure is determined by genetic information that’s inherited from parents.

● This affects secondary and tertiary structure as well, due to interactions between R groups that depend on the order of amino acids.

secondary and tertiary structure as well, due to interactions between R groups that depend on the

Secondary Structure

Regions of the polypeptide chain that are coiled or folded which will eventually contribute to overall shape.

● Result from hydrogen bonds between repeating members of the backbone; this is all about backbone interactions.

● Within the backbone, there is attraction between oxygen and hydrogen that is attached to nitrogen.

between oxygen and hydrogen that is attached to nitrogen. Delicate coil structure held by hydrogen bonds

Delicate coil structure held by hydrogen bonds between every fourth amino acid.

held by hydrogen bonds between every fourth amino acid. 2+ segments of the polypeptide chain lying

2+ segments of the polypeptide chain lying side by side are connected by hydrogen bonds between parts of the 2 parallel segments.

Tertiary Structure ● Overall 3D shape of a polypeptide stabilized by side chain interactions. ●

Tertiary Structure

Overall 3D shape of a polypeptide stabilized by side chain interactions.

● Hydrophobic Interactions: As a polypeptide folds, amino acids with hydrophobic R groups cluster at the core of the protein while avoiding water. Once they’re close, intramolecular forces hold them together.

Hydrogen bonds between polar side chains and ionic bonds between positive/negative side chains help stabilize structure.

● Disulfide Bridges: Covalent, reinforcing bonds that form where 2 cysteine monomers with sulfhydryl groups (-SH) on their R groups are brought close by protein folding. The 2 sulfurs bond, and this bridge rivets 2 regions together.

Quaternary Structure

● Some proteins consist of 2+ polypeptide chains aggregated into one functional macromolecule.

● Overall protein structure resulting from the aggregation of these polypeptide units.

● Not all proteins have this level of structure.

structure resulting from the aggregation of these polypeptide units. ● Not all proteins have this level

Directionality of Proteins

● The orientation of a strand of monomers and polymers.

● The amino acid ends must be placed in a particular direction to code in a certain sequence.

● The order of bases in the chain determines the amino acid sequence for which it codes.

● Where the functional groups are in relation to the protein structure determines its function and when it changes, so does the action of the protein(s)!

in relation to the protein structure determines its function and when it changes, so does the

Denaturation

● If the pH, salt concentration, temperature, or other aspects of the environment are modified, weak chemical bonds that are very important to protein structure may fall apart.

● Without its specific shape, a protein cannot carry out its biological function.

● If transferred to a nonpolar solvent, hydrophobic interactions will fall apart and nonpolar regions will face outward.

● Can sometimes return to its previous state (renature) when the denaturing agent is removed from the environment.

● Can sometimes return to its previous state (renature) when the denaturing agent is removed from

Proteins!!!!!!

Proteins!!!!!! KAHOOT
Proteins!!!!!! KAHOOT
Proteins!!!!!! KAHOOT