Molecules Unit 1 Test

State

Give the answer

Describe

Give characteristics

Distinguish

Give differences

Compare

Similarities + differences

Explain

Give the reason or mechanism

Nucleic Acids contain what elements

Carbon, Hydrogen, Oxygen, Phosphorous, and Nitrogen

What is the monomer and polymer of a nucleic acid

Nucleotide, polynucleotide.

Bond types in nucleic acids

Hydrogen bonds between nitrogenous bases, covalent bonds for strand backbones, and glycosidic bonds, which are covalent bonds bonding the nitrogen base and the pentose sugar.

Carbohydrates contain what elements

Carbon, Hydrogen, oxygen

What is the monomer and polymer of a carbohydrate

Monosaccharides, polysaccharides.

Bond types in carbohydrates

Covalent bonds between molecules, known as glycosidic bonds.

Lipids contain what elements

Carbon, hydrogen, and oxygen.

What is the monomer and polymer of a lipid

Fatty acids and glycerol, and triglycerides, phospholipids, steroids, and waxes.

Bond types in lipids

Covalent bonds between carbons, hydrogen, and oxygen.

Proteins contain what elements

Carbon, Hydrogen, Oxygen, Sulfur, and Nitrogen.

What is the monomer and polymer of a protein

Amino acid, and a peptide chain.

Bond types in proteins

Covalent peptide bonds, hydrogen bonds, ionic interactions, hydrophobic interactions, London dispersion forces, and occasionally, disulfide bonds.

DNA structure

Double helix formed by nucleotides, with a sugar phosphate backbone, and nitrogenous bases in the middle. Runs antiparallel, with one strand being 3’ to 5’, and the other being 5’ to 3’.

DNA function

Acts as the blueprint for the body, allows the body to make more cells and acts as the genetic information.

RNA structure

Single strand formed by nucleotides, with a sugar phosphate backbone, and nitrogenous bases on one side.

RNA function

Is essential in transcription and translation, and acts as the genetic information for some organisms.

Cellulose structure

Made of beta glucose, which alternates. It makes long chains which form layers, with hydrogen bonds between each layer making for a stronger structure.

Cellulose function

Acts as the cell wall for plant cells, very durable and strong, keeps in plant’s internal water pressure.

Amylose structure

Made of straight lines of alpha glucose.

Amylose function

Helps make up starch, which is the primary form of energy storage in plants.

Amylopectin structure

Made of straight lines of alpha glucose with occasional branching, every 24-30 single carbon branches. It branches off with a bond coming from the 6th carbon, making a new chain.

Amylopectin function

Helps make up starch, which is the primary form of energy storage in plants.

Glycogen structure

Made of straight lines of beta glucose, with branches every 8-12 single bonds. It acts as a bunch of strands surrounding one glycogenin protein.

Glycogen function

Acts as the primary form of energy storage in animals, with many branches to allow for easy access to monosaccharides.

Triglyceride structure

Made of one glycerol molecule and three fatty acid chains.

Triglyceride function

Stores excess energy.

Phospholipid structure

Made of one glycerol molecule, one phosphate group, and two fatty acid chains, in a hydrophobic head, and a hydrophilic tail.

Phospholipid function

Makes up cell walls and controls what goes in or comes out.

Polarity

When a molecule has a slightly negative and a slightly positive side, making it slightly charged. This makes it soluble in water or other polar or charged substances. This happens in water because oxygen is very electronegative, so it pulls electrons closer to itself than to hydrogen.

Properties of water

Cohesion, adhesion, high specific heat and latent heat of vaporization. It is also known as the universal solvent, since it can dissolve basically sanything that is charged or polar.

Anabolism

The creation of molecules, requiring energy.

Catabolism

When molecules are broken down, releasing energy.

Condensation reaction

When two molecules are combined by removing two hydrogens and one oxygen, making water as a byproduct.

Hydrolysis

When a molecule is broken down through the addition of water.

Glycoproteins

Extensions on the phospholipid bilayer that help act as receptors and signalers, by allowing cells to communicate with each other.

Steroids

Lipids that attach to cell receptors and act as chemical signalers.

Cholesterol

A lipid found in the cell membranes of animal cells, which helps regulate permeability, helps signaling proteins, and keeps the membrane from becoming too fluid at high temperatures.

Sex hormones

Steroids that regulate reproduction and affect, like testosterone or estrogen.

Protein denaturation

When proteins are outside of their optimum pH or temperature, their shape changes permanently, making them useless.

Origin and retention of water

Water came from earth, where it was heated and pushed out as steam, and then it condensed into oceans. It also came from asteroids and meteors. It stays on the planet because of our atmosphere, which causes it to freeze once it gets too high and cold, dropping back down in the form of clouds or snow.

Search for extraterrestrial life

We look for planets in the goldilocks zone of their solar systems, and with water, since water has a high specific heat capacity, can dissolve many things, supports membrane formation, and causes many reactions.

5’ to 3’ directionality of DNA/RNA

DNA has antiparallel strands. Not much else to talk about.

Purine-to-pyramidine pairing

Purines, A and G, always pair with pyramidines, T and C, through hydrogen bonds. A and T use 2 hydrogen bonds, while G and C use 3.

Hershey-Chase experiment

Used two groups of bacteriophage, one with protein coats tagged with sulfur 35, and the other with DNA tagged with phosphorous 32. When they had children, it was found that the descendants of the DNA tagged bacteriophage also had radioactive DNA, while the other bacteriophage didn’t have any radioactive protein coats. This shows that DNA is the genetic information of organisms.

Chargaff’s DNA base data

He extracted DNA, broke it down, and used chromatography to find the amount of each nitrogenous base in DNA. He found that A and T had the same amount, and so did G and C.

Nucleosome

A DNA strand wrapped around 8 histone proteins, with an additional histone tying the group together.

Structure of an Amino Acid

Amine group (NH2), alpha carbon attached to a hydrogen, a carboxyl group (COOH), and an R group.

Difference between L and D amino acids

L amino acids have their amine group on the left side when drawn a standard way. D amino acids have it switched, with the amine group being on the right side.

Amino acid R groups

Variable part of amino acids, can be neutral, polar, charged, acidic, or basic.

Polar amino acids

They are polar if their R groups contain oxygen and nitrogen, which are electronegative, making the amino acid slightly charged and letting hydrogen or ionic bonds form.

Acidic Amino Acids

Their R group has a carboxylic group (COOH) and loses its hydrogen atom, becoming negatively charged.

Basic Amino Acids

If the R group has a positive charge, and contains nitrogen and resemble ammonia, they are usually basic.

Non-polar amino acids

R groups with no electronegative atoms are non-polar, with no hydrogen bonds.

Primary Proteins

Single polypeptide chain, no folding. Covalent bonds only.

Secondary structure

Local folding, caused mostly by hydrogen bonds. These hydrogen bonds happen regualrly between the N-H of one amino acid, and the C=O on another one. Alpha helixes and beta pleated sheets.

Tertiary structure

More 3D, folded shape, with ionic bonds between charged R groups, covalent bonds between R groups, hydrogen bonding between R groups, and some hydrophobic and hydrophilic interactions of R groups. Disulfide bonds can also exist.

Quaternary structure

Like tertiary, but with more polypeptide chains. It can have hydrogen bonds, covalent bonds, ionic bonds, and hydrophilic and hydrophobic interactions for bonding.

Conjugated proteins

A protein, usually quaternary, attached to a non-polypeptide group, known as a prosthetic group. An example is hemoglobin.

Non-conjugated proteins

Proteins that are only made up of polypeptides.

Globular proteins

Rough, compact, rounded proteins. Usually soluble in water, act as catalysts, transport, and signaling. Hemoglobin is an example.

Fibrous proteins

Long, extended branches or fibres. They are usually insoluble in water, and help with structure and support. An example is keratin in hair or collagen in skin.