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AP Biology Vocab

Macromolecules

TermDefinition
hydrophilic water loving
hydrophobic water fearing
atoms building blocks of matters
bonding when two nuclei attract the same electrons
ionic bond transfer of electrons, the one that gains and electron, anion (-)
covalent bond electrons are shared by two atoms, results in a molecules
electronegativity is a measure of how strongly atoms attract bonding electrons to themselves
non-polar molecules balanced and symmetrical due to equal sharing of electrons, created non-charged molecules
polar unbalanced due to unequal sharing electrons thus it confers a partial charge to the molecule
ions charged particles resulting from the giving or taking of electrons
hydrogen bonding between partial positive hydrogen and partial negative oxygen of adjacent molecule
lipids do not form true polymers; are hydrophobic because they consist of hydrocarbons
Glycerol a 3-carbon alcohol with a hydroxl group attached to each carbon
unsaturated fatty acid have one or more double bonds
hydrocarbons are organic molecules consisting of only carbon and hydrogen
functional groups are the chemical groups that affect molecular function by being directly involved in chemical reactions
seven functional groups ▪ Hydroxyl group -OH ▪ Carbonyl group >C=O ▪ Carboxyl group -COOH ▪ Amino group -NH2 ▪ Sulfhydryl group -SH ▪ Phosphate group -OPO3-2 ▪ Methyl group -CH3
polymer is a long molecule consisting of many similar building blocks
monomers small building-block molecules
dehydration reaction occurs when two monomers bond together through the loss of a water molecule
hydrolysis a reaction that is essentially the reverse of the dehydration reaction
carbohydrates include sugars and the polymers of sugars
monosaccharides have molecular formulas that are usually multiples of CH20; glucose is the most common monosaccharide
disaccharide is formed when a dehydration reaction joins two monosaccharides; this covalent bond is called a glycosidic linkage
polysaccharides, the polymers of sugars, have storage and structural roles; the structure and function of a polysaccharide are determined by its sugar monomers and the positions of glycosidic linkages
starch, aka amylose an energy storage polysaccharide of plants, consists entirely of glucose monomers
glycogen is a (short term energy) storage polysaccharide in animals
cellulose is a major component of the tough wall of plant cells ▪ Like starch and glycogen, cellulose is a polymer of glucose, but the glycosidic linkages in cellulose differ ▪ The difference is based on two ring forms for glucose
chitin another structural polysaccharide, is found in the exoskeleton of arthropods ▪ Chitin also provides structural support for the cell walls of many fungi ▪ Polysaccharide Summary: Starch-storage in plants Glycogen- storage in animals Cellulose- struc
phospholipid, two fatty acids and a phosphate group are attached to glycerol
two types of nucleic acids Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA)
nucleic acids are polymers called polynucleotides; each polynucleotide is made of monomers called nucleotides
pyrimidines include cytosine (C), thymine (T), and uracil (U) – single ring
purines include adenine (A) and guanine (G) – double ring
antiparallel the two backbones run in opposite 5'→ 3' directions from each other, an arrangement
double helix DNA molecules have two polynucleotides spiraling around an imaginary axis
protein functions defense, storage, transport, cellular communication, movement, and structural support
polypeptides are unbranched polymers built from the same set of 20 amino acids
protein is a biologically functional molecule that consists of one or more polypeptides
amino acids are organic molecules with carboxyl and amino groups
four levels of protein structure ▪ Proteins are very diverse, but have three levels of structure called primary, secondary, and tertiary structure ▪ A fourth level, quaternary structure, arises when a protein consists of two or more polypeptide chain
primary structure primary structure of a protein is its unique sequence of amino acids, held by peptide bonds between amino acids
secondary structure found in most proteins, consists of coils and folds in the polypeptide chain, due to hydrogen bonds
tertiary structure is the 3-D globular form determined by interactions among various side chains (R groups), held by various bonds, Hydrogen bonds, disulfide bridges, van der Waal interactions, hydrophobic interactions and ionic bonds
quaternary structure results from interactions between multiple polypeptide chains, due to all the same bonds seen in the tertiary structure.
chaperonins are protein molecules that assist the proper folding of other proteins
denaturation loss of a protein’s native structure
Created by: goelesh000
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