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AP Biology- Biochemistry

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macromolecule

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Biology Science

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Mar 1, 2020

Cards (87)

Section 1

(50 cards)

macromolecule

Front

giant molecule formed by the joining of smaller molecules

Back

carbonyl

Front

carbon double bonded to oxygen; ketones and aldehydes

Back

monomer

Front

the subunit that serves as the building block of a polymer.

Back

hydroxyl

Front

hydrogen bonded to oxygen bonded to an organic molecule's carbon skeleton; alcohol; polar

Back

enzyme

Front

catalytic protein that lowers a reaction's energy of activation

Back

peptide bond

Front

bond creating amino acid chains or polymers

Back

salt

Front

an ionic compound which is made up of two groups of oppositely charged ions.

Back

polymer

Front

long molecule consisting of many similar or identical monomers linked together

Back

tertiary structure

Front

overall 3D conformation; determines function

Back

allosteric regulation

Front

the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site

Back

induced fit model

Front

enzyme model where the substrate induces the enzyme to alter its shape slightly so it fits better

Back

saturated fat

Front

fat without double bonds

Back

evaporative cooling / heat of vaporization

Front

property of a liquid where the surface becomes cooler during evaporation due to the loss of molecules

Back

purine

Front

adenine and guanine; six-membered ring fused to a five-membered ring

Back

monosaccharide

Front

C6H12O6 simple sugar; glucose, galactose, and fructose

Back

polar

Front

electrons shared unequally

Back

covalent bond

Front

bond resulting from the sharing of electrons

Back

nonpolar

Front

electrons shared equally

Back

cofactor

Front

inorganic chemical compound or metallic ion that is required for an enzyme's activity

Back

secondary structure

Front

a specific region of a protein formed with hydrogen bonds- beta pleated sheet or alpha helix

Back

beta pleated sheet

Front

secondary structure form of a protein; spider webs and silk

Back

surface tension

Front

measure of how difficult it is to stretch or break the surface of a liquid

Back

coenzyme

Front

organic molecules that are required by certain enzymes to carry out catalysis (vitamins)

Back

competitive inhibition

Front

compounds that look like the normal substrate compete for the same active site on the enzyme

Back

disulfide bridge

Front

tertiary structure; strong covalent bond formed when one sulfur of one cysteine monomer bonds to the sulfur of another

Back

carboxyl

Front

oxygen double bonded to a carbon atom that is bonded to a hydroxyl group

Back

alpha helix

Front

secondary structure form of a protein; human hair (keratin)

Back

cohesion

Front

attractive forces between molecules of the same substance

Back

ionic bond

Front

bond resulting from a transfer of electrons

Back

metabolism

Front

sum of all chemical reactions that take place in cell

Back

quaternary structure

Front

protein with more than one polypeptide chain

Back

functional group

Front

components of organic molecules most often involved in chemical reactions

Back

buffer

Front

substance that resists changes in pH

Back

unsaturated fat

Front

fat with double bonds

Back

isomer

Front

organic compounds with the same molecular formula but different structure

Back

sulfhydryl

Front

sulfur bonded to hydrogen in roughly the shape of a hydroxyl; cysteine

Back

pyrimidine

Front

cytosine, thymine, and uracil; six-membered ring

Back

van der Waals interactions

Front

tertiary structure; weak attractions between molecules or parts of molecules that result from localized charge fluctuations

Back

primary structure

Front

linear sequence of amino acids; peptide bonds

Back

fatty acid

Front

hydrocarbon chain with a carboxyl group at one end; majority portion in lipids

Back

hydrophobic interaction

Front

tertiary structure; weak chemical bond formed when molecules that do not mix with water change to exclude the water

Back

chemical equilibrium

Front

when the reaction rate is about the same in either direction

Back

adhesion

Front

attractive forces between unlike molecules

Back

glycerol

Front

alcohol portion of a lipid

Back

hydrocarbon

Front

organic molecule consisting of only hydrogen and carbon

Back

noncompetitive inhibition

Front

a molecule binds to an enzyme somewhere other than the active site and reduces the activity of the enzyme

Back

amine

Front

nitrogen bonded to two hydrogens and to the carbon skeleton

Back

phosphate

Front

phosphorous bonded to four oxygens, two have negative charges, one is bonded to the carbon skeleton; phospholipid

Back

nucleotide

Front

building block of a nucleic acid; five carbon sugar covalently bonded to a nitrogen base and a phosphate group

Back

steroid

Front

lipid with a four fused ring structure; cholesterol and testosterone

Back

Section 2

(37 cards)

cellulose

Front

a structural polysaccharide of plant cell walls, consisting of glucose monomers joined by B glycosidic linkages. A type of plant starch.

Back

phospholipid

Front

a lipid made up of glycerol joined to two fatty acids and a phosphate group. The hydrocarbon chains of the fatty acids act as nonpolar hydrophobic tails, while the rest of the molecule acts s a polar, hydrophilic head. They form bilayers that function as biological membrane.

Back

dehydration synthesis

Front

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

Back

carbohydrate

Front

a sugar (monosaccharide) or one of its dimers (disaccharides) or polymers (polysaccharides). Primarily C, H and O.

Back

nucleotide

Front

the building block of a nucleic acid, consisting of a five-carbon sugar covalently bonded to a nitrogenous base and one or more phosphate groups.

Back

peptide bond

Front

the covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction.

Back

methyl

Front

carbon bonded to three hydrogens; arrangement determines function of male and female sex hormones

Back

polysaccharide

Front

a polymer of many monosaccharides, formed by dehydration reactions.

Back

What are the functions of carbohydrates

Front

function as energy source & structure

Back

denaturation

Front

loss of a proteins normal 3D structure; can possibly be caused by pH and temperature which affect the ionic bonds, hydrogen bonds & hydrophilic interactions

Back

triglyceride

Front

a lipid consisting of three fatty acids linked to one glycerol molecule

Back

hydrolysis

Front

a chemical reaction that breaks bonds between two molecules by the addition of water; functions in dis-assembly of polymers to monomers.

Back

enzyme

Front

a macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction without being consumed by the reaction. most of them are proteins.

Back

hydrophobic

Front

a type of weak chemical interaction caused when molecules that do not mix with water coalesce to exclude water.

Back

fat/oil

Front

a lipid consisting of three fatty acids lined to one glycerol molecule; also called a triacylglycerol or triglyceride. Function as energy storage.

Back

glycogen

Front

an extensively branched glucose storage polysaccharide found in the liver and muscle of animals; the animal equivalent of starch.

Back

saturated

Front

a fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that are attached to the carbon skeleton.

Back

deoxyribose

Front

the sugar component of DNA nucleotides, having one fewer hydroxyl group than ribose, the sugar component of RNA nucleotides.

Back

disaccharide

Front

a double sugar, consisting of two monosaccharides joined by a glycosidic linkage formed by a dehydration reaction.

Back

monosaccharide

Front

the simplest carbohydrate, active alone or serving as a monomer for disaccharides and polysaccharides. Also called simple sugars, they have formulas that are generally some multiple of CH2O (1:2:1).

Back

glycosidic linkage

Front

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

Back

lipids

Front

any of a group of large biological molecules, including fats, phospholipids, and steroids, that mix poorly, if at all, with water (hydrophobic). No true monomers.

Back

protein

Front

a biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific three-dimensional structure.

Back

ribose

Front

the sugar component of RNA nucleotides.

Back

amino acid

Front

an organic molecule possessing both a carboxyl and an amino group. The monomers of polypeptides. There are 20 different forms. Distinguished by side chains.

Back

macromolecule

Front

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

Back

polymer

Front

a long molecule consisting of many similar or identical monomers linked together by covalent bonds.

Back

starch

Front

a storage polysaccharide in plants, consisting entirely of glucose monomers joined by x glycosidic linkages. Used for energy storage.

Back

Functions of proteins

Front

structural support, catalyst, transport, defense, movement, regulation

Back

unsaturated

Front

a faty acid that has one or more double bonds betwen carbons in the hydrocarbon tail. such bonding reduces the number of hydrogen atoms attached to the carbon skeleton.

Back

Four classes of biological macromolecules

Front

Proteins, carbohydrates, nucleic acids, lipids

Back

RNA

Front

transmission of information, consists of monomers with a ribose sugar and nitrogenous bases cytosine (C), guanine (G), adenine (A) & uracil (U). Single stranded.

Back

steroid

Front

a type of lipid characterized by a carbon skeleton consisting of four fused rings with various chemical groups attached. Function as part of membranes or hormones.

Back

polypeptide

Front

a polymer of many amino acids linked together by peptide bonds.

Back

DNA

Front

a nucleic acid molecule, usually a double-stranded helix, in which each polynucleotide strand consists of nucleotide monomers with a deoxyribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G), and thymine (T); capable of being replicated and determining the inherited structure of a cell's proteins.

Back

What are the three types of lipids?

Front

fats/oils, phospholipids & steroids

Back

phosphodiester linkage

Front

bond between nucleotides in nucleotide chain to form polynucleotide

Back