Mcat

Front 1

WATER

Back 1

a solvent in which the chemical reactions of living cells take place

Front 2

HYDROGEN BONDING

Back 2

hydrogen boinding between F, O, N

Front 3

HYDROPHILIC

Back 3

water loving

Front 4

HYDROPHOBIC

Back 4

water fearing

Front 5

HYDROLYSIS

Back 5

when a macromolecule is broken into two smaller molecules through the addition of water

Front 6

DEHYDRATION

Back 6

when two molecules are combined to form a larger molecule and water is formed as a byproduct

Front 7

LIPIDS

Back 7

biological molecules that are essential to life and perform a variety of functions in the body (e.g. fats)

Front 8

FATTY ACIDS

Back 8

besides being lipids themselves, they are the building blocks for most, but not all, complex lipids

Front 9

SATURATED FATTY ACIDS

Back 9

possess only single carbon-carbon bonds

Front 10

UNSATURATED FATTY ACIDS

Back 10

contain one or more carbon-carbon double bonds

Front 11

TRIACYLGLYCEROLS

Back 11

commonly called TRIGLYCERIDES or simply FATS and oil, are constructed from a three carbon backbone called GLYCEROL, which is attached to three fatty acid chains

Front 12

ADIPOCYTES

Back 12

fat cells, whose cytoplasm contains almost nothing but triglycerides

Front 13

PHOSPHOLIPIDS

Back 13

lipids with a phosphate group attached

Front 14

phosphoglycerides

Back 14

built from a glycerol backbone, but a polar phosphate group replaces one of the fatty acids

Front 15

AMPHIPATHIC

Back 15

molecules that have a polar and non-polar end

Front 16

glycolipids

Back 16

have one or more carbohydrates attached to the three-carbon glycerol backbone instead of the phosphate group (as seen in phosphoglycerides)

Front 17

SPHINGOLIPIDS

Back 17

similar to phospholipids(in that they have a long fatty acid chain and a polar head group); however, rather than a glycerol, the backbone molecule is an amino alcohol called a sphingosine

Front 18

sphingomyelin

Back 18

have a phosphate group attached to the sphingosine backbone and is thus a phospholipid, although it is not a phosphoglyceride

Front 19

PHOSPHATIDS

Back 19

another way of describing the glycerol backbone with a phosphate group attached

Front 20

plasmalogens

Back 20

only phosphoglyceride that does not have a phosphatidic acid backbone (which is another way of describing the glycerol backbone with a phosphate group)

Front 21

STEROIDS

Back 21

four-ringed structures

Front 22

terpenes

Back 22

sixth class of lipids that are often part of pigments in the body

Front 23

vitamin A

Back 23

included in terpenes, is important for vision

Front 24

WAXES

Back 24

type of lipid that are formed by an ester linkage between a long-chain alcohol and a long-chain fatty acid

Front 25

eicosanoids

Back 25

20 carbon; include prostagladins, thromboxanes, and leukotrienes

Front 26

PROSTAGLADINS

Back 26

group of lipids made at sites of tissue damage or infection that are involved in dealing with injury and illness.

Front 27

lipoprotein

Back 27

transport insoluble lipids in the blood; contains a lipid core surrounded by phospholipids and apoproteins

Front 28

apoproteins

Back 28

the protein portion of a molecule, as in lipoproteins

Front 29

very low density lipoproteins (VLDL)

Back 29

lipoproteins that have high lipids, low protein

Front 30

low density lipoproteins (LDL)

Back 30

lipoproteins that have more lipids than protein

Front 31

high density lipoproteins (HDL)

Back 31

lipoproteins that have more protein than lipids

Front 32

VITAMINS

Back 32

cannot be produced by the body, therefore they are essential

Front 33

FAT-SOLUBLE VITAMINS

Back 33

vitamin A (terpenes) and vitamin D

Front 34

CARBOHYDRATES

Back 34

biological molecule of importance due to usefulness in energy storage and providing easily accessible energy to the body

Front 35

POLYSACCHARIDESpolysaccharides

Back 35

long chains of carbohydrates

Front 36

MONOSACCHARIDES

Back 36

single sugar molecule

Front 37

HEXOSES

Back 37

six carbon carbohydrates, such as glucose and fructose

Front 38

GLYCOGEN

Back 38

branched glucose polymer with alpha linkages

Front 39

STARCH

Back 39

form of long-term storage of polysaccharides in plants

Front 40

amylose

Back 40

form of starch: may be branched or unbranched and has the same alpha linkage as glycogen

Front 41

amylopectin

Back 41

resembles glycogen but had a different branching structure

Front 42

CELLULOSE

Back 42

structural material formed from glucose molecules in plants

Front 43

NUCLEOTIDES

Back 43

class of molecules involved in the cell's use of energy as well as the building block of every organism's genetic material

Front 44

NUCLEOSIDES

Back 44

consist of the pentose sugar attached to a a nitrogenous base

Front 45

NUCLEIC ACIDS

Back 45

polymers of nucleotides

Front 46

PHOSPHODIESTER BONDS

Back 46

bonds that join nucleotides together into long strands

Front 47

SUGAR-PHOSPHATE BACKBONE

Back 47

when phosphodiester bonds link the phosphate group of one nucleotide and the third carbon of the pentose sugar of the other nucleotide

Front 48

DNA

Back 48

deoxyribonucleic acid

Front 49

ADENINE (A)

Back 49

purine

Front 50

GUANINE (G)

Back 50

purine

Front 51

CYTOSINE (C)

Back 51

pyrimidine

Front 52

THYMINE (T)

Back 52

pyrimidine

Front 53

PURINES

Back 53

two-ringed structure

Front 54

PYRIMIDINES

Back 54

single ring structure

Front 55

WATSON-CRICK model

Back 55

form DNA usually exists in- double helix

Front 56

b form

Back 56

structure of DNA when the two strands lie side by side in opposite 3'--> 5' direction

Front 57

ANTIPARALLEL

Back 57

formal name of double helix structure of DNA in B form

Front 58

DOUBLE STRANDED

Back 58

structure of DNA characteristic of the binding of two strands by hydrogen bonds

Front 59

BASE PAIRING

Back 59

hydrogen bonding between two nuclotides

Front 60

BASE PAIRS (BP)

Back 60

used to measure the length of DNA strand

Front 61

COMPLEMENTARY STRANDS

Back 61

two strands that match bases in the correct order

Front 62

DOUBLE-HELIX

Back 62

structure of DNA formed when two complementary strands bind together

Front 63

RNA

Back 63

ribonucleic acid

Front 64

SINGLE STRANDED

Back 64

usually in RNA molecules, consisting of one strand of nucleotides

Front 65

URACIL (U)

Back 65

pyrimidine; replaces thymine in RNA

Front 66

ATP (ADENOSINE TRIPHOSPHATE)

Back 66

main source of readily available energy for the cell

Front 67

AMINO ACIDS

Back 67

the building blocks of proteins

Front 68

POLYPEPTIDES

Back 68

chain of amino acids linked together by peptide bonds

Front 69

AMIDE

Back 69

an amine connected to a carbonyl carbon

Front 70

SIDE CHAIN

Back 70

the R group that differs between amino acids

Front 71

PRIMARY STRUCTURE

Back 71

single chain- the number and sequence of amino acids in a polypeptide

Front 72

SECONDARY STRUCTURE

Back 72

distinct shapes formed from the single primary polypeptide chain

Front 73

A-HELIX

Back 73

twisted shape of primary polypeptide chain

Front 74

B-PLEATED SHEET

Back 74

shape of primary polypeptide when it lies along itself

Front 75

CONFORMATION

Back 75

overall shape of the protein

Front 76

TERTIARY STRUCTURE

Back 76

3-D shape formed by the curls and folds of the peptide chain

Front 77

CYSTEINE

Back 77

amino acid containing sulfur

Front 78

CYSTINE

Back 78

dimer formed from the oxidation of two cysteine molecules

Front 79

PROLINE

Back 79

induce turns that disrupt both a-helix and B-pleated sheet formation due to its physical structure

Front 80

QUATERNARY STRUCTURE

Back 80

when two or more polypeptides chains bind together

Front 81

native conformation

Back 81

water surround proteins in a biological environment helps stabilize...

Front 82

SOLVATION LAYER

Back 82

organized structure of proteins that force hydrophobic groups toward the inner area of the protein

Front 83

ENTROPY

Back 83

when decreasing the size of the highly ordered solvation layer, it increases the...

Front 84

DENATURED

Back 84

when the native conformation is disrupted

Front 85

globular and structural

Back 85

two types of proteins; more types of globular proteins than structural proteins

Front 86

collagen

Back 86

structural protein made from a unique type of helix, is the most abundant protein in the body

Front 87

glycoproteins

Back 87

proteins with carbohydrate groups attached; component of cellular plasma membrane

Front 88

proteoglycans

Back 88

mixture of proteins and carbohydrates (more than 50%) and are a major component of the extracellular matrix

Front 89

cytochromes

Back 89

require a prosthetic heme group to function in carrying out electron transport via oxidation and reduction of the heme group

Front 90

prosthetic

Back 90

nonproteinaceous

Front 91

heme

Back 91

cofactor containing iron

Front 92

conjugated proteins

Back 92

proteins containing nonproteinaceous components (e.g. cytochromes)

Front 93

MINERALS

Back 93

dissolved inorganic ions inside and outside the cell

Front 94

hydroxyapatite

Back 94

minerals combine and give strength to a matrix such in bone

Front 95

ENZYMES

Back 95

regulate biological reactions

Front 96

CATALYST

Back 96

functioning of enzymes to lower the energy of activation for a biological reaction and thus increasing the rate of that reaction

Front 97

SUBSTRATES

Back 97

the reactant or reactants upon which an enzyme works

Front 98

ACTIVE SITE

Back 98

a particular location where the substrate binds to the enzyme

Front 99

ENZYME-SUBSTRATE COMPLEX

Back 99

the enzyme and the substrate bind together to form...

Front 100

ENZYME SPECIFICTY

Back 100

normally, enzymes are designed to work only on a specific substrate of group of closely related substrates

Front 101

LOCK AND KEY MODEL

Back 101

theory: the active site of the enzyme has a specific shape, like a lock that only fits a specific substrate, the key

Front 102

INDUCED FIT MODEL

Back 102

theory: shapes of both the enzyme and the substrate are altered upon binding

Front 103

SATURATION KINETICS

Back 103

as the relative concentration of substrate increases, the rate of the reaction also increases, but to a lesser and lesser degree until a maximum rate

Front 104

V MAX

Back 104

maximum rate of a reaction proportional to enzyme concentration

Front 105

turnover number

Back 105

the number of substrate molecules one active site can convert to product in a given unit of time when an enzyme solution is saturated with substrate

Front 106

MICHAELIS CONSTANT

Back 106

Km

Front 107

Km

Back 107

the substrate concentration at which the reaction rate is equal to 1/2 Vmax

Front 108

1/2 Vmax

Back 108

half the maximum rate of a reaction proportional to enzyme concentration

Front 109

COFACTOR

Back 109

non-protein component, coenzyme or metal ions used to help enzyme reach optimal activity

Front 110

COENZYMES

Back 110

cofactors that are all organic molecules (e.g. water-soluble vitamins)

Front 111

WATER-SOLUBLE VITAMINS

Back 111

serve as coenzymes or their precursors

Front 112

cosubstrates

Back 112

type of coenzyme that reversibly bind to a specific enzyme and transfer some chemical group to another substrate (e.g. ATP)

Front 113

prosthetic groups

Back 113

type of coenzyme that remain covalently bound to the enzyme throughout the reaction, and, like the enzyme, emerge from the reaction unchanged

Front 114

apoenzyme

Back 114

an enzyme without a cofactor and is completely nonfunctional

Front 115

holoenzyme

Back 115

an enzyme with its cofactor

Front 116

proteolytic cleavage (irreversible covalent modification)

Back 116

when specific peptide bonds on zymogens are cleaved

Front 117

ZYMOGEN

Back 117

or proenzyme, an inactive form of an enzyme

Front 118

reversible covalent modification

Back 118

enzymes are activated or deactivated by phosphorylation or the addition of some modifer

Front 119

control proteins

Back 119

protein subunits that associate with certain enzymes to activate or inhibit their activity

Front 120

calmodulin and G-proteins

Back 120

examples of control proteins

Front 121

ALLOSTERIC INTERACTIONS

Back 121

modification of an enzyme's configuration through binding of an activator or inhibitor at a specific binding site

Front 122

NEGATIVE FEEDBACK (FEEDBACK INHIBITION)

Back 122

one of the products downstream a reaction series comes back and inhibits the enzymatic activity

Front 123

POSITIVE FEEDBACK

Back 123

the product returns to an earlier step to activate the associated enzyme

Front 124

ALLOSTERIC REGULATION

Back 124

products that bind to the enzyme and cause a conformational change

Front 125

ALLOSTERIC INHIBITORS

Back 125

products that bind to the enzyme and cause a conformational change that inhibits the enzyme

Front 126

ALLOSTERIC ACTIVATORS

Back 126

products that bind to the enzyme and cause a conformational change that activates the enzyme

Front 127

POSITIVE COOPERATIVITY

Back 127

the first substrate changes the shape of the enzyme, allowing other substrates to bind more easily

Front 128

NEGATIVE COOPERATIVITY

Back 128

the first substrate changes the shape of the enzyme, making it more difficult for other substrates to bind

Front 129

IRREVERSIBLE INHIBITORS

Back 129

agents that bind irreversibly to enzymes and disrupt there function

Front 130

COMPETITIVE INHIBITORS

Back 130

compete with the substrate by binding reversibly with noncovalent bonds to the active site

Front 131

UNCOMPETITIVE INHIBITORS

Back 131

bind at a site other than the active site, only when enzymes have already bound substrate

Front 132

MIXED INHIBITORS

Back 132

bind at a site on the enzyme other than the active site and thus do not prevent the substrate from binding (can bind to enzyme alone or enzyme-substrate complex)

Front 133

NONCOMPETITIVE INHIBITOR

Back 133

type of mixed inhibitor that bind just as readily to enzyme with a substrate as to those without

Front 134

OXIDOREDUCTASES

Back 134

catalyzes the transfer of electrons or hydrogens ions (oxidation-reduction reactions)

Front 135

TRANSFERASES

Back 135

catalyzes reactions in which groups are transferred from location to another

Front 136

HYDROLASES

Back 136

regulate hydrolysis reactions

Front 137

LYASES

Back 137

catalyze reactions in which functional groups are added to double bonds or, conversely, double bonds are formed via the removal of functional groups (e.g. ATP synthase)

Front 138

ISOMERASES

Back 138

catalyzes the transfer of groups within a molecule, with the effect of producing isomers

Front 139

LIGASES

Back 139

catalyze condensation reactions coupled with the hydrolysis of high energy molecules

Front 140

synthase

Back 140

particular type of lyase that catalyzes the addition of one substrate to the double bond of a second substrate

Front 141

synthetases

Back 141

require energy input from ATP or some other nucleotide

Front 142

kinases

Back 142

an enzyme that phosphorylates a molecule

Front 143

phosphatase

Back 143

an enzyme that dephosphorylates a molecule

Front 144

heterokinase

Back 144

an enzyme that phosphorylates glucose as soon as it enters the cell