Chapter 4 and 5 Biology Test

Isomer Types

Structural, Geometric, Enatiomers

Isomers

Compounds that have the same formulas but different functions.

Structural Isomer

Different in covalent arrangements of their atoms

Geometric Isomer

Same covalent partnership but different in spatial arrangements. Arise from the flexibility of double bonds.

Enantiomers Isomers

Molecules that are mirror images of each other. Usually an asymmetric carbon.

Functional Groups

Groups that alter the function of molecules

Hydrocarbons

Organic compounds that contain only carbon and hydrogen

Hydrolysis

Dehydration process allowing for chemical breakdown

Organic

relating to or derived from living matter

Hydrocarbon Uses

Fuel, high energy

What functional group is this?

Hydroxyl

What does a hydroxyl do when added to a molecule

It makes it polar, or an alcohol if it is on a carbon chain

What functional group is this?

Carbonyl

What are the types of carbonyl groups and how are they different?

When the carbonyl is added to the end of a molecule it forms an aldehyde and if it is added to the middle it forms a ketone

What functional group is this?

Carboxyl

What does a carboxl do when added to a molecuel

It makes it acidic because it is an H+ donor and polar

What functional group is this?

Amino

What does an amino do when added to a molecule

It makes it basic (h+ acceptor)

What functional group is this?

Sulfhydryl

What does a sulfhydryl do when added to a molecule

Creates thiols (compounds that possess a sulfhydryl)

What functional group is this?

Phosphate

What does a phosphate do when added to a molecule

It turns it to a weak acid and is used for energy transfers

What functional group is this?

Methyl

What does a methyl do when added to a molecule

Makes it nonpolar and hydrophobic

What functional group is this?

Acetyl

What does a acetyl do when added to a molecule

Makes it polar and hydrophilic

Macromolecules

Large molecules formed by joining many subunits together. Aka polymers.

Monomer

A building block of a polymer

Dehydration Synthesis

The chemical reaction that joins monomers into polymers. Covalent bonds are formed by the removal of water molecule between the monomers.

Hydrolysis

Reverse of dehydration synthesis. Breaks polymers into monomers by adding water.

Main types of macromolecules

Carbohydrates, Lipids, Proteins, Nucleic Acids

What is the monomer of nucleic acids

Nucleotides

Elements in nucleic acids

Carbon, hydrogen, oxygen, nitrogen, phosphorus (CHONP)

Food sources for nucleic acids

All foods!

Examples of Nucleic Acids

DNA, RNA, ATP

Polymer of nucleotide

Nucleic acid

DNA

Deoxyribonucleic acid, 1 less H+ than RNA

RNA

Ribonucleic acid

Strands of DNA?

Double Stranded

Strands of RNA?

Single Stranded

Parts of Nucleotide?

nitrogenous base, pentose sugar, phosphate

pentose sugar

5-C sugar, ex ribose, deoxyribose

Pyrimidines

Cytosine(C) Thyme(T) Uracil(U) 1 ring

Purines

Adenine(A) Guanine(G) 2 ring

Pyrimidines and purines in DNA

Cytosine(C) Thyme(T) Adenine(A) Guanine(G)

Pyrimidines and purines in RNA

Cytosine(C) Uracil(U) Adenine(A) Guanine(G)

Adenine(A) pairs with ____

Thyme(T) in DNA and Uracil(U) in RNA

Guanine(G) pairs with ____

Cytosine(C)

ATP

Adenosine triphosphate, the source of energy for use and storage at the cellular level

Nucleic Acids

Polymers that contain information

Lipids

Broad group of organic compounds which include fats, waxes, sterols, fat-soluble vitamins, monoglycerides, diglycerides, phospholipids, and others.

Monomer of lipids

Glycerol

Elements in lipids

Carbon, hydrogen, oxygen (CHO)

Function of lipids

Store energy, cushion and insulate organs, material used for cell membrane

Food source for lipids

Butter, nuts, oil

Example of lipids

Fats, Oils, Waxes

Structure of lipids

long hydrocarbon chain with a carboxyl on the end

Name of link between lipids

Ester bonds/linkage(covalent bonds)

Do lipids link together?

No, lipids stack on top of each other. Not true macromolecules.

Saturated fatty acid

All single bonds in the fatty acid tail. Solid at room temp. C5H12

Unsaturated fatty acid

At least one double bond between carbons in fatty acid tail. Liquid at room temp. C5H10

Polysaturated

More than one double bond.

Hydrogenated Oils

Added hydrogen to fatty acid tail.

Elements in carbohydrates

Carbon, hydrogen, oxygen (CHO). 1C:2H:1O

Monomer of carbohydrate

Monosaccharides

Function of carbohydrate

Provide material to build cell membrane. Quick energy for cells.

Foods for carbohydrates

Pastas, breads, fruits, vegetables

Example of carbohydrates

Glucose, Fructose, Lactose, Cellulose

Polymer of Carbohydrate

Polysaccharide

Shape of carbohydrate

Hexagon

Disaccharide

2 monosaccharides linked together

Oligosaccharides

3 to 10 monosaccharides. Used for cell identification and communication

Polysaccharides

100 to 1000 monosaccharides.

Alpha glucose in plants

Starch (Potato), large chains

Alpha glucose in animals

glycogen ( the stored form of glucose that's made up of many connected glucose molecules)

Beta glucose in plants

Cellulose, cell walls

Beta glucose in animals

Chitin, exoskeletons

Steroids

4 fused hydrocarbon rings. Differ by attached functional groups. Ex estrogen, testosterone, cholesterol

Elements in proteins

Carbon, hydrogen, oxygen, nitrogen (CHON)

Monomer of proteins

Amino acid

Function of proteins

Provide structure, aid in muscle movement, provide immunity

Proteins food source

Seafood, milk, eggs, cheese, meat

Examples of proteins

Insulin, hemoglobin, antibodies, enzymes

Polymer of proteins

polypeptide/proteins

Stages of proteins folding

Primary, secondary, tertiary, quaternary

Polypeptide

Multiple amino acids linked together

Dipeptide

Two amino acids linked together

What dictates amino acid order in a polypeptide?

DNA that tells RNA how to make the polypeptide

How many changes does a protein need to go through to become functional?

4, the quaternary stage

Primary protein folding stage

2d line of amino acids made by peptide bonds

Secondary protein folding stage

3d structure formed by hydrogen bonding between the R groups. Two main secondary structures. Either forms an alpha helix or beta pleated sheet, determined by the hydrogen bonding pattern of the amino acids in the polypeptide chain.

Tertiary protein folding stage

Bonding between the R groups. Possible bonds: Ionic bonds, disulfur bridges, vanderwaal’s bonds, hydrophobic interactions.

Quaternary protein folding stage

When two or more polypeptides bond together. The molecule becomes functional.

Events causing a proteins to lose it’s shape

Ph shifts, high salt concentrations, heat