AP Biology Biochemistry

AP Biology Biochemistry

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Section 1

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butter, lard

Front

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Mar 1, 2020

Cards (106)

Section 1

(50 cards)

butter, lard

Front

Give two examples of saturated fats

Back

monomer

Front

the subunit that serves as the building block of a polymer

Back

no true polymers, mix poorly with water, consist mostly of hydrocarbon regions

Front

What three characteristics do all lipids share in common?

Back

sugars starches

Front

Carbohydrates include _______ and _________

Back

hydrogenated oil

Front

hydrogen is added to vegetable oils to change the oil from liquid to solid.

Back

saturated fat

Front

type of fat that consists of all single bonded carbons and lots of hydrogens, solid at room temperature, commonly found in animal fats

Back

sucrose

Front

table sugar

Back

olive oil, canola oil

Front

Give two examples of unsaturated fats

Back

maltose

Front

malt sugar

Back

dehydration synthesis

Front

the process in which two molecules become covalently bonded to each other with the removal of a water molecule

Back

glucose + fructose

Front

What two monomers make up sucrose?

Back

glucose + galactose

Front

What two monomers make up lactose?

Back

chitin

Front

structural polysaccharide that gives many bugs their exoskeleton

Back

lysis

Front

root word meaning to break

Back

polymer

Front

a long molecule consisting of many similar or identical building blocks linked by covalent bonds

Back

isomers

Front

Compounds with the same formula but different structures.

Back

cows, termites, fungi

Front

Give three organisms that can digest cellulose

Back

glycosidic linkage

Front

A covalent bond formed between two monosaccharides by a dehydration reaction.

Back

ester linkage

Front

the bond between a fatty acid and a glycerol that forms a lipid

Back

trans fat

Front

An unsaturated fat, formed artificially during hydrogenation of oils, containing one or more trans double bonds.

Back

carbohydrates, lipids, proteins, nucleic acids

Front

Name the four major classes of large molecules in living things

Back

hydro

Front

root word meaning water

Back

cellulose

Front

structural polysaccharide that comprises plant cell walls

Back

water

Front

To summarize, when two monomers are joined, a molecule of _____ is always removed

Back

enzymes that are able to digest starch by hydrolyzing alpha linkages are unable to hydrolyze the beta linkages of cellulose because of the distinctly different shapes

Front

Why can you not digest cellulose?

Back

three fatty acids, one glycerol molecule

Front

A fat is composed of _____ and _______

Back

macromolecule

Front

giant molecule formed by the joining of smaller molecules, usually by a dehydration reaction

Back

Carbon-1 of glucose has bonded with Carbon-4 of glucose

Front

What does 1-4 glycosidic linkage mean in terms of carbon numbering?

Back

monomer

Front

Is glucose a monomer or a polymer?

Back

energy storage, structural

Front

Name the two types of polysaccharides

Back

starch

Front

Has 1-4 Beta glucose linkages

Back

unsaturated fat

Front

type of fat that contains a double bonded carbon that causes a bend in structure, commonly found in plants, liquid at room temperature

Back

hydrolysis

Front

the process in which a water molecules added to a polymer in order to break down bonds between two molecules

Back

long term energy storage, insulation, padding, absorb vitamins

Front

List four important functions of fats

Back

glucose

Front

What is this?

Back

fats, waxes, oils, phospholipids, steroids

Front

What are the five categories of lipids?

Back

ketone sugar

Front

Carbohydrate: carbonyl group located within the skeleton

Back

lipids

Front

What is the one class of large molecules that does not include macromolecules?

Back

C6H12O6

Front

Give the formula for glucose

Back

monosaccharides

Front

The monomer of carbohydrates

Back

-ose

Front

Root word meaning "full of"

Back

the molecules can't pack close together to solidify due to double bond bend

Front

Why are many unsaturated fats liquid at room temperature?

Back

carbonyl, hydroxyl

Front

All sugars have the same two functional groups, name them

Back

disaccharide

Front

A double sugar, consisting of two monosaccharides joined by dehydration synthesis.

Back

cellulose, chitin

Front

Give two types of polysaccharides used as structural

Back

lactose

Front

milk sugar

Back

glycogen

Front

is a storage polysaccharide produced by vertebrates that is stored in your liver

Back

starch, glycogen

Front

Give two types of polysaccharides used in energy storage

Back

aldehyde sugar

Front

Carbohydrate: carbonyl group located at the end of skeleton

Back

glucose + glucose

Front

What two monomers make up maltose?

Back

Section 2

(50 cards)

hydrophilic, hydrophobic

Front

Phospholipids has ______ heads, and ________ tails

Back

nerve cell receptors

Front

Give an example of a receptor protein

Back

insulin

Front

Give an example of a hormonal protein

Back

sugar, nitrogenous base, phosphate group

Front

What are the three components of a nucleic acid

Back

cholesterol

Front

What is this?

Back

amino acid

Front

the monomer of a protein

Back

secondary

Front

Level of protein sequence: hydrogen bonds between repeating constituents in backbone, determined by backbone

Back

helix, pleated sheet

Front

What are the two types of secondary protein structure?

Back

cholesterol, vertebrate sex hormones

Front

Give two examples of a steroid

Back

keratin

Front

Give an example of a structural protein

Back

5' to 3'

Front

Always read mRNA from -- to ---, the end is always with an OH

Back

sickle-cell disease

Front

occurs when there is a change, specifically from glutamic acid to valine acid, in the amino acid sequence in the primary structure of the protein

Back

hydrocarbons

Front

Nonpolar amino acid side chains typically contain ______

Back

nucleic acid

Front

any of various macromolecules composed of nucleotid chains that are vital constituents of all living cells

Back

storage

Front

Type of protein: stores amino acids

Back

digestive enzymes

Front

Give an example of an enzymatic protein

Back

structural

Front

Type of protein: support

Back

tertiary structure

Front

Level of protein sequence:

Back

nucleotide

Front

A building block of DNA, consisting of a five-carbon sugar covalently bonded to a nitrogenous base and a phosphate group.

Back

dipeptide bond

Front

two amino acids put together

Back

tertiary

Front

Level of protein sequence: regions repel and attract each other, determined by interactions in R groups

Back

mRna is synthesized in the nucleus, mRNA moves into cytoplasm via nuclear pore, a protein is synthesized by a ribosome by using the correct info carried on mRNA

Front

Give the three detailed steps in which the flow of genetic information is achieved from DNA to RNA to proteins in a cell

Back

antibodies

Front

Give an example of a defensive protein

Back

chaperonins

Front

protein molecules that assist the proper folding of other proteins

Back

quaternary structure

Front

Level of protein sequence:

Back

casein

Front

Give an example of a storage protein

Back

amino acid

Front

What is this?

Back

hemoglobin

Front

Give an example of transport protein

Back

cytosine, adenine, thymine, guanine

Front

What four nitrogenous bases are found in DNA

Back

the side chain

Front

What is represented by the R group in an amino acid?

Back

hormonal

Front

Type of protein: coordinates organism activities

Back

contractile and motor structural

Front

Type of protein: movement

Back

Hydrocarbons

Front

What are the "tails" of phospholipids made up of which make them hydrophobic?

Back

primary structure

Front

Level of protein sequence:

Back

charged side chains

Front

Electrically charged amino acid side chains typically contain ____________

Back

peptide bond

Front

the covalent bond between the carbonyl group on one amino acid and the amino acid group on another, formed through dehydration reaction

Back

polypeptide

Front

the polymer of a protein

Back

defensive

Front

Type of protein: protects against disease

Back

receptor

Front

Type of protein: response of cell to chemical stimuli

Back

20

Front

How many different types of amino acid side chains are there?

Back

quaternary

Front

Level of protein sequence: two or more polypeptides form into one functional macromolecule

Back

primary

Front

Level of protein sequence: basic amino acid sequence, determined by DNA

Back

actin, myosin

Front

Give two examples of the contractile and motor structural proteins

Back

heat, pH, salts

Front

Give three ways a protein may become denatured

Back

transport

Front

Type of protein: transports substances

Back

denaturation

Front

a process in which a protein loses its native shape due to the disruption of weak chemical bonds and interactions, becoming biologically inactive

Back

enzymatic

Front

Type of protein: accelerates chemical reactions

Back

secondary structure

Front

Level of protein sequence:

Back

OH or SH groups

Front

Polar amino acid side chains typically contain _______

Back

amphipathic

Front

a molecule that has hydrophobic regions and hydrophilic regions

Back

Section 3

(6 cards)

cytosine, adenine, uracil, guanine

Front

What four nitrogenous bases are found in RNA

Back

nitrogenous bases

Front

In DNA, what molecules are said to be the "rungs" on the double helix model

Back

cytosine, adenine, uracil, guanine

Front

What four nitrogenous bases are found in RNA

Back

deoxyribose lacks one less oxygen on the second carbon

Front

What is the difference between ribose and deoxyribose

Back

double helix

Front

The form of native DNA, referring to its two adjacent polynucleotide strands wound into a spiral shape.

Back

antiparallel

Front

The two sugar-phosphate backbones run in opposite 5'-3' directions in DNA which is why it is said to be ______________

Back