Chapter 5- The structure and Function of Large Biological Molecules

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Last updated 4:41 PM on 9/17/26
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67 Terms

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Biomolecules

The organic molecules that are essential to living organisms

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The 4 primary classes of biomolecules

1) Carbohydrates

2) Proteins

3) Nucleic Acids

4) Lipids

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Monomers

Single, individual building blocks that can be repetitively linked together to form polymers

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Monomers vary?

Depending on the type of biomolecule polymer

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Consistent and not consistent monomers

Carbohydrates, Proteins and nucleic acids use consistent monomers to form polymers, but lipids do NOT

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Dehydration Synthesis

Forms covalent bonds to link individual monomers and build a polymer

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Hydrolisis

Breaks covalent bond to break down a polymer

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Carbohydrates

Carbon-based-molecules hydrated with many hydroxyl groups (-OH)

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What is carbohydrates referred to

Saccharides

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Simple Carbohydrates

Fit Cn(H2O)n formula exactly

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Complex Carbohydrates

Can differ slightly from Cn(H2O)n and can have P,N or S atoms

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Monosaccharide

A single carbohydrate unit or monomers

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Oligosaccharide

2 to 20 covalently linked monosaccharides

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Polysaccharides

More than 20 covalently linked monosaccharides (polymer)

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Glycosidic Bonds

Covalent bonds that link monosaccharides together

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Hydrolysis

Breaks down polysaccharides into individual monosaccharides

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What are the two main functions of a carbohydrate

Storage Support: Helps build

Energy Storage: Used for short-term energy-storage

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Cellulose

Most abundant carbohydrate found in plant-cells

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Starch

Storage form of glucose in plants

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Chitlin

Found in the exoskeleton of a insect or crustaceans

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Glycogen

Storage form of glucose in animals

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Proteins

A class of biomolecule polymers made of amino acid monomers

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Peptide Bonds

Covalent bonds linking adjacent amino acids together

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Proteins polymers have directionality

N-terminal and C-terminal Ends

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Amino Acids

The monomers of proteins

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Amino Acids: Nonpolar Side Chains; Hydrophobic

Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, Proline (9)

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Amino Acids: Electrically charge side chains; hydrophilic

Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine (6)

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Amino Acids: (Negatively Charged)

Aspartic Acid, Glutamic acid

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Amino Acids: (positively charged)

Lysine, Arginine, Histidine

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1st protein related term

Amino Acids: A single protein unit or monomer

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2nd protein-related terms

Oligo peptide: 2 to 20 covalently linked amino acids

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3rd Protein related terms

Peptide: Less than 50 covalently linked amino acids

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4th Protein-related terms

Polypeptide: Greater than 50 covalently linked amino acids

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5th Protein-related terms

Protein: One or multiple polypeptide chains in their folded/functional forms

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Primary Protein Structure

Types, quantity, and order of amino acids. Determines all other levels of structure

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Secondary Protein structure

Formation of either alpha-helics or Beta-sheets in the protein backbone

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Tertiary protein structure

Overall 3D-shape of a polypeptide chain

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Quaternary Protein structure

Multiple polypeptide chains associate to form a single, functional protein

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Why is a proteins structure and shape critical

Its critical for its proper function

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Denatured Protein

A non-functional protein that has altered its shape

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What causes a denatured protein

pH, Temp, or salt concentration

Chaperone Proteins

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Chaperone Proteins

Proteins that help other proteins can re-form their shape (or renature)

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Nucleic acids

A class of biomolecule polymers that store/ encode genetic information

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Directionality of the nucleic acid polymer

5’ and 3’ ends

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Nucleotide monomers consist of 3 components

1) Phosphate Group

2) Pentose Sugar

3) Nitrogenous base

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Nitrogenous Basses: Pyrimidines

Single-ringed molecules

Cytosine, Thymine, Uracil

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Nitrogenous Bases: Purines

Double Ringed Molecules

Adenine, Guanine

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Nitrogenous bases on different DNA strands pair together

A with T and C with G

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Phosphodiester Bonds

The covalent bonds that link nucleotides together

Results in the sugar-phosphate “Backbone”

Directionality of 5’ phosphate end to 3’ hydroxyl end

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Deoxyribonucleic acid (DNA)

Stores genetic/hereditary information in the cell.

Forms a double-helix 2 anit-parallel strands connected by base-pair hydrogen bonds

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Ribonucleic acid (RNA)

Has a variety of functions including acting as a template for synthesizing proteins

Usually forms a single-stranded nucleotide chain

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Lipids

Hydrophobic biomolecules insoluble in water that are highly diverse in their structure and function

Can be amphipathic: Having both hydrophobic and hydrophilic group

Do not form polymers

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Lipids include

Fats, oils, phospholipids, steroids, and waxes

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Fats and oils

Long term energy storage in animals and plants

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Phospholipids

Major component of cell membranes

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Steroids

Component of plasma membrane and hormones

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Waxes

Protection and prevention of water loss

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Fatty acids

Hydrocarbon chains of varying length with a carboxylic acid

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Saturated Fatty acids

Fully saturated with hydrogens (only contains C-C single bonds)

Solids at room temp

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Unsaturated Fatty acids

Not fully saturated with hydrogens due to presence of more than 1 C=C double bond

-Double bond creates a bend in the chain making them liquids at room temp

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Trans-fat

Artificial unsaturated fatty acids that are NOT bent (linear)

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Triglycerides

A lipid with 3 fatty acid chains covalently linked to a single glycerol molecule

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Fatty acids linked to glycerol results in

Dehydration synthesis reactions

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Phospholipids

Large class of lipids that contain a phosphate group

Major component of all cell membranes

Amphipathic molecules with a hydrophilic head and hydrophobic tails

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Steroids

Lipids that are made of 4 fused carbon ring structures

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Cholesterol

Common steroid important for the structure of animal cell membranes

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Waxes

Another class of lipid that can be used for protection and prevention of water loss