Mmbio 240 Exam 1

Front 1

Schrodinger

Back 1

A physicist who emphasized the importance of the chromosome

Front 2

Crick

Back 2

the leader of molecular biology

Front 3

How do bacteria exchange DNA?

Back 3

through pili

Front 4

Do viruses have linear or circular DNA?

Back 4

linear

Front 5

What's the order of organisms relative to amount of DNA?

Back 5

Eukaryotes>bacteria>phages

Front 6

What makes a phosphodiester bond?

Back 6

nucleoside triphosphate
sugar-o-p-o-sugar

Front 7

what type of bond makes one dimensional structures?

Back 7

covalent

Front 8

what type of bond makes three dimensional structures?

Back 8

noncovalent

Front 9

Mulder

Back 9

chemical characteristic of proteins

Front 10

Sumner

Back 10

crystallogrophied proteins and enzymes to find that enzymes are proteins

Front 11

Pauling

Back 11

discovered the alpha helix
peptide bond
secondary protein structure
nature of genetic diseases

Front 12

Sanger

Back 12

sequenced amino acid chains for proteins (insulin)

Front 13

Perutz

Back 13

x-ray crystallography showed that proteins are 3D (especially hemoglobin)

Front 14

What amino acid can form disulfide bonds?

Back 14

cysteine

Front 15

What two amino acids are known for forming beta-turns?

Back 15

proline and glycine

Front 16

Anfinsen

Back 16

stated that 3D structure is determined by primary structure

Front 17

What's a lysate?

Back 17

a mixture of disrupted cells

Front 18

What's coomasie?

Back 18

a blue dye used to make proteins visible

Front 19

Which Amino Acids have Side Chains with basic groups?

Back 19

Lysine, Arginine, Histidine

Front 20

Which Amino Acids have Side Chains with Acidic Groups?

Back 20

Aspartic Acid, Glutamic Acid

Front 21

Which Amino Acids have Side Chains with Polar but Uncharged Groups?

Back 21

Serine, Threonine, Tyrosine, Asparagine, Glutamine, Cysteine

Front 22

Which Amino Acids have Side Chains with Nonpolar Groups?

Back 22

Glycine, Alanine, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan, Methionine, Proline

Front 23

What’s so weird about Proline?

Back 23

The R group loops around and connects with the amine in the peptide backbone, this prevents that bond from rotating like it would with other peptide backbones

Front 24

What is x-ray crystallography used for?

Back 24

It determines the structure of a protein

Front 25

-What’s so weird about Proline?

Back 25

- The R group loops around and connects with the amine in the peptide backbone, this prevents that bond from rotating like it would with other peptide backbones

Front 26

Gel Electrophoresis

Back 26

the basic process by which molecules are moved through an electrified matrix. The direction of motion of the molecules depends on the charge.

Front 27

primary antibodies

Back 27

- attach themselves to the protein of interest

Front 28

secondary antibodies

Back 28

- attach themselves to another antibody usually has an enzyme attached to the end that make detection of the protein easier

Front 29

SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis)

Back 29

-SDS stands for sodium docecyl sulfate its function is to denature proteins by coating them with negative charges

Front 30

-DTT

Back 30

stands for dithoithreitol which reduced agents that break disulfide bonds (re-natures proteins)

Front 31

BME

Back 31

stands for mercaptoethanel which reduced agents that break disulfide bonds (re-natures proteins)

Front 32

standard polyacrylamide gel

Back 32

a gel that is submerged in buffer with an electric current running through it to separate the different proteins, creates a two dimentional result

Front 33

chelated nickel column

Back 33

another way to filter out proteins by adding a hexahistidine to a protein to make it able to attach itself to a nickel column

Front 34

immunoprecipitation

Back 34

binding specific antibodies to the beads so that certain proteins will stick to them and let everything else pass through.

Front 35

What category does yeast fall into?

Back 35

eukaryote

Front 36

Gel electrophoresis

Back 36

the basic process by which molecules are moved through an
electrified matrix. The direction of movement depends on the charge of the molecules,
and rate of movement depends on the size of the molecules (smaller=faster)

Front 37

isoelectric point:

Back 37

pH at which protein reaches neutral charge

Front 38

What characterized the mmbio revolution?

Back 38

boldness, imagination, models, and reductionism

Front 39

Carl Woese

Back 39

Tree of Life

Front 40

Shrodinger

Back 40

wrote What is Life? and started the scientific revolution that resulted in mmbio. physicist.