Biochemistry Exam 1 Bchm561

Front 1

Structure of Adenine and symbol

Back 1

see notes

Front 2

Structure of Guanine

Back 2

see notes

Front 3

Structure of Thymine

Back 3

notes

Front 4

Structure of Cytosine

Back 4

Notes

Front 5

Structure of Uracil

Back 5

Notes

Front 6

Bonding Between Base Pairs Adenine and Thymine

Back 6

Notes
(2 hydrogen bonds)

Front 7

Bonding Between Base Pairs Guanine and Cytosine

Back 7

Notes
(3 Hydrogen Bonds)

Front 8

Drawing of Covalent Structure of DNA

Back 8

see notes
alternating sugar-phosphate groups
bases attached to sugar.

Front 9

If 2 molecules had a tendency to associate with each other through hydrogen bonds, what would be the effect of putting them into water?

Back 9

Because of its high dielectric constant and its ability to form competing hydrogen bonds, the interaction between the 2 molecules would be weakened

Front 10

Noncovalent Interactions that contribute to the formation of the DNA double helix

Back 10

electrostatic interactions
hydrogen bonding
van der waals forces
hydrophobic effect

Front 11

Proteins are linear polymers built of monomers called:

Back 11

amino acids

Front 12

Proteins contain a wide range of

Back 12

functional groups

Front 13

Only _ Amino Acids constitute proteins

Back 13

L (S rather than R)

Front 14

Amino acids with large hydrocarbon side chains (3):

Large hydrocarbon side chains means that they are:

Back 14

Valine
Leuchine
Isoleuchine*

hydrophobic

Front 15

Contain nonpolar aliphatic side chains(6):

Aliphatic side chains means that they are:

Back 15

Glycine
Alanine
Valine
Leucine
Isoleucine*

Methionine (contains thioether side group)

Proline (forms a ring with the alpha carbon)

Hydrophobic

Front 16

Amino acids with simple aromatic side chains (3)

(hydrophobic?)

Back 16

Phenylalinine

Tyrosine (one reactive -OH group)

Tryptophan

Phenylalanine is strictly hydrophobic while Tryptophan and Tyrosine are less so because of their hydroxyl and NH groups

Front 17

Amino acids that are polar but uncharged:

a) contain OH groups attached to an aliphatic side chain

b) Unchanged derivatives of the acidic amino acids (2)

c)other

Back 17

a) Serine and Threonine* contain hydroxyl groups on an aliphatic side chain

[Serine = alanine with an OH]
[Threonine = valine with OH]

b)Asparagine (derivative of Aspartate)
Glutamine (derivative of Glutamate)

Asparagine and Glutamine contain a terminal Carboxylamide in placeo of a carboxylic acid

The side chain of glutamine is one methylene group longer than that of asparagine.

c)Cysteine(structurally similar to serine but contains a sulfhydryl or thiol group in place of the hydroxyl)

may come together to form disulfide bonds-important for stabilizing proteins.

Front 18

2 amino acids with complete charges that render them highly hydrophilic
-have relatively long side chains that terminate with groups that are positively charged at a neutral pH

Back 18

Lysine
Arginine

Front 19

Contains an aromatic ring that can be positively charged

often found:

Back 19

Histidine

the imidazole group (aromatic ring) can be uncharged or positively charged near neutral pH

in the active sites of enzymes

Front 20

Charged, hydrophilic set of amino acids with acidic side chains

Back 20

aspartic acid and glutamic acid(aspartate andglutamate)

usually lack a proton present in the acid form and hence are negatively charged.