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Biochemistry Flashcards

Midterms

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1
Q

the study of life processes, structures mechanism, reaction of the molecular levels

A

biochemistry

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2
Q

removal of carboxyl group of organic acids

A

decarboxylation

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2
Q

occurs when it gains oxygen or loses hydrogen

A

oxidation

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3
Q

addition of phosphate group

A

phosphorylation

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3
Q

takes place in the presence of oxygen

A

aerobic oxidation

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3
Q

reverse of oxidation

A

reduction

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3
Q

occurs in the absence of oxygen

A

anaerobic oxidation

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3
Q

defined as polyhydroxyaldehides or ketones or compound which produce them on hydrolysis

A

carbohydrates

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3
Q

addition of acyl group

A

acetylation

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3
Q

union of a substance with one or more water molecules

A

hydrolysis

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3
Q

simple fragments unite with one another to form a more complex compound

A

condensation

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3
Q

transfer of amino group

A

transamination

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3
Q

transfer of a methyl group

A

transmethylation

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3
Q

living matter is composed of mainly 6 elements

A

carbon, hydrogen, oxygen, nitrogen, phosphorus, sulfur

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3
Q

chemicals or molecules that are present in living organism

A

biomolecules

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4
Q

the most predominant and versatile element of life

A

carbon

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4
Q

french term of carbohydrates

A

hydrate de carbone

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4
Q

functions of carbohydrates

A

most abundant source of energy, storage of energy, cell growth and fertilization, protection layer for animal and plants

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5
Q

the compounds that have the same structural formula but differ in their spatial configuration

A

stereoisomers

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5
Q

the simplest group of carbohydrates and are often referred to as simple sugars

A

monosaccharides

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5
Q

an important character of monosaccharides

A

stereoisomerism

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6
Q

used to represent the stereoisomers that are not mirror images of one another

A

diastereomers

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6
Q

are a special type of stereoisomers that are mirror images of each other

A

enantiomers

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7
Q

meaning of d

A

Dextrorotatory

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7
Q

meaning of L

A

Levorotatory

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8
Q

the cyclic isomers differing from each other in configuration at anomeric carbon

A

anomers

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8
Q

defined as an atom in a molecule that is bonded to four different chemical species allowing for optical isomerism

A

chiral center

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9
Q

two sugars that differs in configuration at only 1 chiral center

A

epimers

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9
Q

it oxidizes glucose to gluconic acid

A

nitric acid

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9
Q

loosely defined group of molecules; water insoluble and soluble in organic solvents; hydrophobic; chief concentrated storage form of energy forming about 3.5% of the cell content

A

lipids

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9
Q

greek word of lipids

A

lipos-fat

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9
Q

reaction wherein the silver metal forms deposits and acts like a mirror; a qualitative test for glucoce

A

silver mirror test

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10
Q

lipids composed of what elements?

A

carbon, hydrogen, oxygen

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10
Q

follows the same mechanism as mentioned for the tollen’s reagent

A

fehling’s solution

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10
Q

building blocks of lipids

A

fatty acids, glycerol

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10
Q

double bonds joining the carbon atoms in the hydrocarbon tails

A

unsaturated

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10
Q

have just one carbon-carbon double bond

A

monounsaturated

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10
Q

functions of lipids

A

concentrated fuel reserve of the body, regulates the membrane permeability, source of fat soluble vitamins, cellular metabolic regulators, protect internal organs

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10
Q

these are carboxylic acids typically contain between 12 to 20 carbon atoms

A

fatty acids

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10
Q

have only single bonds joining the carbon atoms in their hydrocarbon tails

A

saturated fatty acids

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10
Q

simplest trihydric alcohol

A

glycerol

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10
Q

have two or more double bonds

A

polyunsaturated

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10
Q

able to pack closely together with one another, interacting with one another, interacting with one another through london force

A

hydrocarbon tails of saturated fatty acids

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11
Q

ester of fatty acids with alcohol

A

simple lipids

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11
Q

esters produced by combining fatty acids with long chain alcohols 14-16 carbon atoms

A

waxes

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11
Q

animals fats and vegetable oils are triglycerides

A

fats and oils

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12
Q

triglycerides composed of how many fatty acids?

A

3 fatty acids

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12
Q

double bonds can be broken to produce small organic molecules that have unpleasant odors

A

oxidation

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13
Q

made by combining glycerol, two fatty acids, one phosphate group and one alcohol molecule

A

glycerophospholipids

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13
Q

lipids that are composed of fatty acids, alcohol and an additional group, the prosthetic group

A

complex (compound) lipids

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13
Q

double bonds are removed by adding hydrogen with a presence of hydrogen

A

catalytic hydrogenation

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13
Q

the alcohol in this group of phospholipids

A

sphingosine

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13
Q

also known as soap making; hydrolysis of ester groups in the presence of OH-

A

saponification

14
Q

obtained on the hydrolysis of group 1 and 2 lipids which possess the characteristics of lipids

A

derived lipids

14
Q

contains a fatty acids, carbohydrate and nitrogenous base

A

glycolipids

14
Q

macromolecular complexes of lipids with proteins

A

lipoproteins

14
Q

long-chain lipids that are components of many biologically important pigments, such as chlorophyll and the visual pigment retinal ex: rubber

A

terpenes

14
Q

found in membranes composed of four carbon rings

A

steroids

15
Q

local hormones; tissue hormones

A

eicosanoids

15
Q

gives rise to three major classes of eicosanoids; released on demand from the cell membrane

A

arachidonic acid

16
Q

3 major classes of eicosanoids

A

prostaglandins. thromboxanes. leukotrienes

17
Q

indicates that the enzyme cyclizes arachidonic acid that is it converts part of the molecules to a close-ring; incorporates oxygen into molecule

A

cyclooxygenase

18
Q

catalyzes the reactions of arachidonic acid to leukotrienes A4

A

lipoxygenase

18
Q

has a ketone on its ring

A

prostaglandin e2

19
Q

functions of eicosanoids prostaglandins

A

mediator or pain, inducing fever, mucus protection, vasodilation (increased renal blood flow) in kidney, uterine contraction, motility

19
Q

hydroxyl group and form a single bond to a carbon atom

A

prostaglandin f2

19
Q

function of prostacyclin pgi2

A

vasodilation decreased platelet aggregation

20
Q

functions of thromboxanes

A

vasoconstriction increased platelet aggregation

20
Q

function of leukotrienes b4

A

chemotaxis

20
Q

function of leukotrienes c4 and so on.,

A

eosinophils (bronchoconstriction

21
Q

most abundant molecule in the living organism; makes up 50% of the dry weight of the cell

A

proteins

22
Q

greek word or protein meaning holding the first place

A

proteios

22
Q

in 1838 used the term proteins for the high molecular weight nitrogen rich and most abundant substances present in animals and plants

A

mulder

22
Q

functions of proteins

A

movement, structure and support, cellular communication, digestion, transport or oxygen

23
Q

suggested the name proteins to the group of organic compound

A

berzelius

23
Q

5 major elements in proteins

A

carbon, hydrogen, oxygen, nitrogen, sulfur

23
Q

group of organic compounds containing two functional groups amino acid and carboxyl

A

amino acids

24
Q

most common amino acids

A

α-amino acids

24
Q

the most common α-amino acids

A

L-α-amino acids

24
Q

substances containing equal numbers of positive and negative charge-due to their carboxyl and amine group

A

zwitterions

24
Q

contains a carboxyl group

A

polar acidic

24
Q

side chain is alkyl an aromatic ring

A

non polar

25
Q

usually an alcohol or a phenol

A

polar neutral

25
Q

another name for amide bond

A

peptide bond

25
Q

contains amino group

A

polar basic

25
Q

between α-amino and v-carboxyl group

A

amide bond

25
Q

the end of the peptide chain with the unreacted amino group

A

N-terminus

25
Q

the end of the peptide chain with the free carboxyl group

A

C-terminus

25
Q

made up of one or more polypeptide chain; can be classified as being either fibrous or globular

A

proteins

25
Q

exists as long fibers or strings; usually tough and water insoluble, such as collagen and keratin

A

fibrous proteins

25
Q

spherical in shape, highly folded and tend to be water soluble

A

globular proteins

25
Q

type of proteins

A

fibrous, globular, membrane, disordered

25
Q

some proteins contain chemical groups other than amino acids

A

conjugated proteins

26
Q

functions of proteins additional

A

enzyme, transport, nutrient and storage, contractile and motile, structural, defense, regulatory

26
Q

caused by disruption of the non covalent forces responsible for maintaining the native conformation

A

denaturation

26
Q

factors that can caused denaturation

A

changes in temperature or pH, agitation, use of soaps or detergent

26
Q

used to find out the amount of protein in biological fluids and foods

A

Kjeldahl’s method

26
Q

molecule that reacts or can be an acid and base

A

ampotheric

26
Q

give protein precipitate that turn flesh to red

A

millon’s test

26
Q

alkaline solution of proteins will give rose pink to violet to purple color

A

biuret test

26
Q

will give violet ring at the point of contact of the two solution

A

hopkin’s cole reaction

27
Q

will give yellow to orange color when neutralized with NaOH

A

Xanthoproteic reaction

28
Q

when solid protein is boiled in concentrated HCl with few drops of sucrose solution

A

Lieberman’s test

29
Q

will produce black precipitate

A

test for the SH group

30
Q

produce violet ring if glycoprotein is present

A

Molisch’s test

31
Q

protein boiled with triketohydrindene hydrate

A

ninhydrin reaction

32
Q

protein deficiency

A

kwashiorkor

33
Q

simplest protein

A

glycine

34
Q

coined the term catalysis (greek to dissolve)

A

berzelius

34
Q

used the word enzyme (greek: yeast) to indicate the catalysis taking place in the biological systems

A

Kuhne

35
Q

he named the active principle of zymase

A

Buchner

35
Q

found contain a mixture of enzymes which could convert sugar to alcohol

A

zymase

36
Q

first achieved the isolation and crystallization of the enzyme urease from jack bean and identified it as a protein

A

James sumner

37
Q

defined as a substance that increases the velocity or rate of a chemical reaction

A

catalysts

37
Q

biocatalyst; the catalyst of life; may be defined as biocatalysts synthesized by living cells

A

enzymes

38
Q

addition or removal of water, ammonia, CO2

A

lyases

39
Q

involved in oxidation-reduction reactions

A

oxidoreductases

39
Q

hydrolysis of various compounds

A

hydrolases

39
Q

synthetic reactions (greek: ligate- to bind) where two molecules are joined together and ATP is used

A

ligases

40
Q

transfer of functional groups

A

transferases

41
Q

isomerization reactions

A

isomerases

41
Q

Factors affecting enzyme activity

A

concentration of enzymes, substrate, effect of temperature, pH, product concentration, activators, time, and light and radiation

41
Q

the metal is not tightly held by the enzymes and be exchanged easily with other ions

A

metal-activated enzymes

41
Q

these enzymes hold the metals rather than tightly which are not readily exchanged

A

metalloenzymes

42
Q

optimum temperature for most of enzymes is between_____

A

35°C-40°C

42
Q

inactivated enzyme

A

apoenzyme

42
Q

coenzymes

A

cofactor

43
Q

formula of holoenzyme

A

inactivated enzyme + coenzyme

44
Q

fit together

A

lock and key hypothesis

45
Q

prevent enzyme from bonding; blocking the active side

A

competitive inhibitor

45
Q

changes shape to fit in the substrate: adjustment bind tightly

A

induced fit hypothesis

46
Q

distort the shape; dumidikit sa enzyme

A

non-competitive inhibitor

Psychology (4 decks)

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