Proteins

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Types of Tissues

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NAR database

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ENZYMES

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Food groups

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Peptide Bond

• the linkage of 2 amino acids

Polypeptide (primary structure)

• a chain of amino acids connected by peptide bonds
• also known as primary structure

Secondary Structure

• takes the primary structure and folds in different ways
• small folded shapes within a protein caused by hydrogen bonding between peptide bonds in the same polypeptide

Tertiary Structure

• finally forms a whole 3D tertiary structure
• larger folded shape of the protein caused by different intermolecular forces of attraction between side chains of amino acids in the same polypeptide.

Quaternary Structure

• when multiple proteins are linked together in their folded tertiary structure.
• some proteins only function when they combine with other protein subunits --> Ex. microtubules, enzymes, actin, myosin, and hemoglobin
• actin and myosin change shape to allow parts of cells or whole organisms to move

Proteins

• the molecules that drive chemical reactions in living things
• the shape of a protein is determined by the type of intermolecular force of attraction between monomers in the protein.
• proteins are found in a variety of food (Ex. meat, fish, beans, seeds, eggs, and nuts)
• proteins are made up of amino acids

Chemical Signalling

• a function of proteins
• signals can travel from one cell to another, or across the whole human body through the bloodstream
• Ex. the body's biochemical response to stress

Nervous System

Neurotransmitters

• Ex. dopamine
• chemical signals produced by neurons

Endocrine System

Hormones

• Ex. adrenaline
• chemical signals produced by glands

Essential Amino Acids (9)

• there are 9 essential amino acids
• these are amino acids that do not occur naturally in our bodies and must come from or diet
• each essential amino acid has an R-group: a part of the chemical structure that differs from other amino acids
• includes: histidine, isoleucine, lysine, methionine, phenylalanine, threonine, tryptophan, leucine and valine

• describes the ability to interact with water
• polar
• includes: histidine, lysine, threonine

• describes the inability to interact with water
• non-polar
• includes: isoleucine, leucine, methionine, phenylalanine, tryptophan, and valine

Non Essential Amino Acids (11)

• there are 11 amino acids that do not classify as essential because we have them naturally within our bodies
• each amino acid has an R-group: a part of the chemical structure that differs from other amino acids
• includes: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine glycine, proline, serine, and tyrosine

Hydrophilic (water loving)

• describes the ability to interact with water
• polar
• includes: arginine, asparagine, aspartic acid, glutamic acid, glutamine, serine, and tyrosine

Hydrophobic (water fearing)

• describes the inability to interact with water
• non-polar
• includes: alanine, cysteine, glycine, and proline