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metabolism Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

electron exchange

A

either by transferring electrons from one atom to another; sharing electrons between atoms

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2
Q

ionic chemical bond

A

formed when electrons are donated by one atom to another

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3
Q

covalent chemical bond

A

formed when two atoms share a pair of electrons

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4
Q

polar covalent bond

A

if one atom is more electronegative than the other the electron is shared unequally

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5
Q

bond length

A

attractive and repulsive forces are in balance when nuclei separated by defined distance

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6
Q

bond strength

A

measured by amount of energy needed to break that bond expressed in kilocalories

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7
Q

double bond

A

four electrons can be shared; 2 coming from each atom

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8
Q

ions

A

molecules carrying plus or minus charges

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9
Q

hydrophobic

A

molecules are uncharged and form few or no hydrogen bonds and do not dissolve in water

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10
Q

acids

A

substances that release protons to form H30+ when they dissolve in water

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11
Q

bases

A

alkaline; substance that accepts protons to form OH-

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12
Q

chemical bond strength

A

in water-kcal; covalent-90, ionic-3, hydrogen-1, van der waals-0.1

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13
Q

electrostatic attraction

A

form between permanent dipoles-polar covalent; fully charged ions- ionic bonds

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14
Q

isomer

A

molecules with the same chemical formula but different structures

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15
Q

optical isomer

A

molecules that are mirror image pairs

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16
Q

sugar groups

A

multiple hydroxyl groups, either one aldehyde or ketone group

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17
Q

sucrose

A

disaccharide of glucose and fructose

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18
Q

condensation reaction

A

molecule of water is expelled as a bond is formed between OH group on one sugar to OH group on another sugar

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19
Q

hydrolysis

A

molecule of water is consumed; two monosaccharides are formed

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20
Q

glycoprotein

A

smaller oligosaccharides are covalently linked to proteins

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21
Q

glycolipid

A

smaller oligosaccharides are covalently linked to lipids

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22
Q

fatty acid

A

hydrophylic carboxylic acid head; hydrophobic hydrocarbon chain

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23
Q

saturated tail

A

no double bonds between carbon atoms

24
Q

triacylglycerol

A

consist of three fatty acid chains joined to a glycerol molecule

25
Q

phospholipid

A

cell membrane; 2 fatty acid tails; glycerol joined to phosphate group which is joined to hydrophilic polar group

26
Q

glycosidic bond

A

covalent bond between two sugar molecules

27
Q

amphiphilic

A

molecules with both hydrophobic and hydrophilic regions

28
Q

common amino acids

A

20 commonly found amino acids with n-amino beginning and c-carboxyl terminus

29
Q

L-form proteins

A

opitcal isomer form found in all eukaryotic protiens

30
Q

catabolism

A

break down food stuff generating energy

31
Q

anabolic

A

biosynthetic; drive the synthesis molecules

32
Q

second thermodynamic law

A

isolated system; the degree of disorder only increases

33
Q

entropy

A

amount of disorder in a system is quantified and expressed as this

34
Q

first thermodynamic law

A

energy can be converted but never created or destroyed

35
Q

oxidation

A

one molecule loses an electron

36
Q

reduction

A

one molecule gains an elecron

37
Q

free energy

A

measures the portion of a systems energy that can perform work

38
Q

free energy change

A

^ is change; ^G=^H-T^S

39
Q

enthalpy

A

symbolized by H; total energy in a system

40
Q

entropy

A

the randomness or disorder of a system

41
Q

spontaneous reaction

A

enthalpy must decrease or entropy must increase

42
Q

exergonic reaction

A

net release of free energy; ^G is negative, cellular respiration is example

43
Q

endergonic reaction

A

absorbs free energy; molecule synthesis

44
Q

energy coupling

A

the use of an exergonic reaction to power an endergonic reaction

45
Q

enzyme active site

A

substrate is held there by hydrogen bonds and ionic bonds

46
Q

cofactor

A

nonprotein helpers; may be bound tightly to enzyme or reversibly with substrate

47
Q

coenzyme

A

if cofactor is organic; such as vitamins

48
Q

competitive inhibitor

A

reduce the productivity of enzymes by blocking substrates from active sites

49
Q

competitive overcome

A

increase the concentration of substrate so that active sites become available

50
Q

noncompetitive inhibitors

A

bind to another part of the enzyme and impede enzymatic reactions

51
Q

irreversible enzyme inhibitors

A

often toxins and poisons that bind covalently

52
Q

allosteric regulation

A

proteins function at one site is affected by the binding of a regulatory molecule at a separate site

53
Q

enzyme cooperativity

A

binding of one substrate to active site locks all subunit active sites in active conformation

54
Q

allosteric inhibitor

A

stabilizes inactive form for one or if multiple subunits all active sites

55
Q

allosteric activator

A

stabilizes active form for one or if multiple subunits all active sites

56
Q

feedback inhibition

A

allosteric regulation where metabolic pathway is switched off by binding of product to early enzyme in the pathway

Biology (28 decks)

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