Chemistry Vocab For Exam 2

Front 1

which has sour taste acid or base?

Back 1

acid

Front 2

which has bitter taste acid or base?

Back 2

base

Front 3

who proposed the first successful concept of acid and base? and what did he say.

Back 3

Arrhenius, he defined acids and bases in terms of the effect of these substances have on water..acids increase H+ ion in water and bases increase OH- ion in water

Front 4

HCL is an acid or base?

Back 4

acid

Front 5

NaOH is an acid or base?

Back 5

base

Front 6

Hydronium ion

Back 6

H3O+

Front 7

what is the formation of hydronium ion?

Back 7

the oxygen in water has unshared pair of electrons. Oxygen uses one pair of unshared electron to form an additional bond with a third hyrogen

Front 8

carboxylic acids are acids or bases

Back 8

acids

Front 9

What did Johannes Bronsted and Thomas Lowry say about acid and base?

Back 9

acid and base reactions can be seen as proton-transfer reactions

Front 10

Acid

Back 10

proton donor (H+ donor)

Front 11

Base

Back 11

proton acceptor (OH- acceptor)

Front 12

amines are acids or bases

Back 12

bases

Front 13

where does proton come from in amines?

Back 13

when an amine is placed is dissolved in water, the proton comes from water and OH- gets left behind

Front 14

define pKa (equilibrium constant for reversible reaction)

Back 14

the tendency of any acid (HA) to lose a proton and form its conjugate base (A-)

Front 15

buffer

Back 15

a combination of substances...usually a weak acid and its conjugat base...that act together to prevent a drastic change in ph when either another acid or base is added

Front 16

chiral carbon atom

Back 16

a carbon bonded to four different groups

Front 17

enantiomers or optical isomers

Back 17

two mirror-image forms of a chiral molecule

Front 18

stereoisomers

Back 18

isomers that have the same molecular and structural formala, but different spatial (3-D) arrangements of their atoms

Front 19

all molecules with chiral center are what?

Back 19

optically active

Front 20

amphoteric (ampholytes)

Back 20

substances having dual nature

Front 21

isoelectric point

Back 21

the ph at which a sample of an amino acid has equal numbers of + and - charges

Front 22

zwitterion

Back 22

when an amino acid is dissolved in water, it exists in solution as the dipolar ion

Front 23

amino terminal (N-terminal)

Back 23

the amino acid with the free alpha amino group at the end of a protein

Front 24

carboxyl terminal (C-terminal)

Back 24

the amino acid with the free alpha carboxyl group at the end of a protein

Front 25

primary structure

Back 25

a description of the colvalent backbone of a polymer (macromolecule), including the sequence of monomeric subunits and any interchain and interchain colvanlent bonds

Front 26

secondary structure

Back 26

the residue by residue conformation of the backbone of a polymer

Front 27

tertiary structure

Back 27

the 3-D conformation of a polymer in its native folded state

Front 28

quaternary structure

Back 28

the 3-D structure of a multisubunit protein; particularly the manner in which the subunits fit together

Front 29

peptide bond

Back 29

amide linkage between the alpha carboxyl of one amino acid and the alpha amino group of another amino acid

Front 30

amphipathic compounds

Back 30

contain regions that are polar(or charged) and regions that are nonpolar

Front 31

hydrophobic

Back 31

the forces that hold the nonpolar regions of the molecules together

Front 32

globular proteins

Back 32

water soluble proteins whose chain is folded in a compact shape with hydrophilic groups on the outside

Front 33

native protein

Back 33

a protein with the shape (sec.,tertiary,quaternary structure) in which it exists naturally in living organisms

Front 34

simple protein

Back 34

a protein composed only of amino acids

Front 35

conjugated protein

Back 35

a protein that incorporates one or more non-amino acid units in its structure

Front 36

fibrous protein

Back 36

tough, insoluble proteins whose protein chains form fibers or sheets; they are composed mainly of either alph helices or B sheets

Front 37

denaturation

Back 37

the loss of secondary, tertiary, or quaternary structure due to disruption of noncovalent interactions and/or disulfide bonds which causes loss of function of the protein

Front 38

what are peptides

Back 38

are linear polymers of amino acids connected by peptide bonds

Front 39

what are proteins

Back 39

are linear polymers of amino acids connected by peptide bonds

Front 40

hydrophobic interaction

Back 40

the force that holds nonpolar molecules together

Front 41

ionic interaction

Back 41

the interaction between charged side chains of amino acids

Front 42

list the 5 hydrophobic aminos

Back 42

valine, alanine, leucine, isoleucine, phenylalanine

Front 43

list the 4 ionic interaction aminos

Back 43

aspartic acid and lysine(attractive) and glutamic acid and aspartic acid (repulsive)

Front 44

what is the function of oxytocin?

Back 44

affects uterine smooth muscle, increase frequency and duration during uterine contraction

Front 45

what is the function of vassopressin?

Back 45

increases water resorption in the kidney

Front 46

what can disrupt alpha helix stability?

Back 46

a sequence of - or + charged amino acids

Front 47

what 2 aminos occur in B turns?

Back 47

glycine-cause its small & flexible
proline-cause cis peptide and tight turns

Front 48

name the 5 class of fibrous proteins

Back 48

keratins,elastins,fibrin,myosins,and collagens

Front 49

name the 5 globular proteins

Back 49

insulin, ribonuclease, immunoglobins, hemoglobin, and albumins

Front 50

Name 3 major buffer systems in the vertebrates?

Back 50

bicarbonate buffer system, phosphate systme, and proteins

Front 51

name 10 aminos that are int the body?

Back 51

valine,methionine,leucine, isoleucine,threonine,lysine, arginine,histidine, phenylalanine,tryptophan