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CHEM 103 > CH 18 > Flashcards

CH 18 Flashcards

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1
Q

Amino acids contain…

A

acidic grp -COOH

basic grp -NH3

can undergo intramolecular acid-base RXN

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2
Q

Zwitterion

A

Neutral dipolar ion that has one (+) charge and one (–) charge

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3
Q

acid- base properties

-zwitterions, amino acids have physical properties w/ salts…….and those are…

A
  • can form crystals
  • high melting points
  • soluble in water but not hydrocarbon solvents
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4
Q

What is the isoelectric point?

A

pH @ which 2 amino acids exists as a zwitterion

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5
Q

In acidic solution (low pH)…

A

Amino acids zwitterions accept protons on their basic -COO- groups

acidic= has positive charge

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6
Q

In a basic solution (high pH)…

A

Amino acid zwitterions lose protons from their acidic -NH3+ groups

basic has negative charge

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7
Q

Chiral

A

having right or left handedness w/ two different mirror images = doesn’t match

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8
Q

Achiral

A

opposite of chiral having superimposable mirror images and thus no right or left handedness

SYMMETRY= achiral

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9
Q 
CHIRAL OR ACHIRAL?
CHAIR
BABY POWDER BOTTLE
SPOON
SCISSORS
A

CHAIR-chiral

BABY POWDER BOTTLE-chiral

SPOON- achiral

SCISSORS- chiral

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10
Q

Molecular handedness and amino acids

A
  • when a carbon has four different groups, it becomes a chiral carbon atom- or chiral center
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11
Q

Enantiomers (optical isomers)

A

two mirror image forms of a chiral molecule

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12
Q

Steroisomers

A

isomers that have the same molecular and structural formula but different spatial arrangements

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13
Q

How many amino acids are chiral out of the 20? Which one is the exception?

A

19 out of 20

Glycine

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14
Q

Primary PRO structure

A

sequence in which amino acids are linked by peptide bonds in a PRO

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15
Q

Primary PRO structure combining

A

a pair of amino acids can be combined to form 2 different dipeptides

-when combining as a product you get H20 and amino acid residue

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16
Q

how are peptides and PRO always written?

A

w/ amino-terminal amino acid on the LEFT

carboxyl- terminal amino acid on the RIGHT

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17
Q

Residue

A

and amino acid unit in a polypeptide bond

18
Q

Hydrogen bonds along the backbone…

A

cause a sheet or helix shape

19
Q

Hydrogen of R groups with each other or with back bone atoms…

A

can cause FOLDING over of THE SHEET OR HELIX

20
Q

Ionic attraction b/t R groups

A

Salt bridges

similar to H+ of R groups w. each other or backbone atoms

21
Q

Hydrophobic interxns b/t R groups

A

create a H20 free “pocket” to carry H20 insoluble substances thru H20

22
Q

Covalent sulfer-sulfer bonds

A

can loop or tie chains together

23
Q

Secondary PRO structure

A

regular and reporting structural patterns
ex:
alpha helix, Beta sheet
-created by hydrogen bonding b/t backbone atoms in neighboring segments of PRO chains

24
Q

Alpha (a) helix…

A

SECONDARY PRO structure in which a PRO chain forms a right-handed coil stabilized by H+bonds b/t peptide groups along backbone

-ex: telephone wire
clockwise coil from ‘C’ terminal

25
Q

Beta (B) sheet

A

SECONDARY PRO struct. in which adjacent PRO chains either in the same molecule or in diff. molecules are held together by H+ bonds along the backbones –>forming flat street structure

Ex: little fan unfolded

26
Q

Secondary PRO structure classified as.

A

globular

fibrous

27
Q

Fibrous PRO

A 
tough
insoluble PRO whose PRO chains form fibers or sheets
ex:
nails
hair
wool
skin
wood
spider web
28
Q

Globular PRO

A

WATER SOLUBLE PRO whose chain is folded in a compact shape w/ HYDROPHILIC grapes on the outside

ex:
eggs
milk
cheese
insulin
29
Q

Tertiary PRO structure

A

the way in which an entire PRO chain is coiled and folded into specific 3D shape

30
Q

Native PRO

A

PRO w/ the shape (secondary, tertiary, & quaternary) which it exists NATURALLY in living organism

31
Q

Simple PRO

A

PRO compose of ONLY amino acids

32
Q

Conjugated PRO

A

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

33
Q

Quaternary PRO structure

A

the way in which TWO or MORE PRO chains aggregate to form LG, ordered structures
EX:
HEMEGLOBIN

34
Q

Collagen

A

Fibrous PRO
most abundant of all PROs in mammals
MAJOR constituent of skin, tendons, bones, blood vessels, and other connective

35
Q

PRO denaturation

A

LOSS of secondary, tertiary, quaternary PRO structure due to disruption of noncovalent interns and/or disulfide bonds that leaves peptide bonds and PRIMARY STRUCTURE INTACT

When PRO denatured ONLY PRIMARY STRUCTURE REMAINS!

36
Q

Chemical Properties of PRO

Heat

A

Disrupts the weak side chain intern

FRYING AN EGG= IRREVERSIBLE

37
Q

Chemical Properties of PRO

Mechanical agitation

A

whipping air bubbles into a foam- air is held in place by disrupted protein

WHIPPING EGGS/ CREAM

38
Q

Chemical Properties of PRO

Detergents

A

disrupt HYDROPHOBIC side chain

DAWN, AJAX

39
Q

Chemical Properties of PRO

Organic Compounds

A

polar solvents can interfere w/ H+ bonds

40
Q

Chemical Properties of PRO

pH change

A

can disrupt salt bridges

MILK SOURING

41
Q

Chemical Properties of PRO

Inorganic salts

A

can disrupt salt bridges

Na+CL-

42
Q

Curling/ straightening hair w/ hot plates…?

A

Reversible denaturing

CHEM 103 (4 decks)

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