Ch 4

Question 1

what is the structure of an amino acid

Answer 1

amino (NH3), Hydrogen, carboxyl(COO), R-group

Question 1

If amino acid has a negative charge what group should it be in?

Answer 1

acidic

Question 2

If amino has a negative charge which group

Answer 2

basic

Question 3

If there is no charge variation what group is it in

Answer 3

non-polar

Question 4

If it has an oxygen or looks like it could interact with water like has a SH/Se waht is it

Answer 4

polar

Question 5

What do chains of amino acids get linked together by?

Answer 5

peptide bonds

Question 6

what kind of reaction is it when amino acids join

Answer 6

condensation reaction (aka dehydration synthesis) (water leaving)

Question 7

WHat is the N-terminus?

Answer 7

the amino acid end, there IS directionality

Question 8

What do we call amino acids when they’re linked together

Answer 8

residues

Question 9

difference between peptide and polypeptide

Answer 9

peptide(below 50) are shorter

Question 10

What is the antisense strand?

Answer 10

the template for RNA polymerase during transcription. it is the one that is read. 3’ to 5’

Question 11

What is the coding or sense strand

Answer 11

the one that is the same as the RNA.

Question 12

What are open reading frames

Answer 12

areas of DNA that actually encode for a gene, the coding region between start and stop codon

Question 13

What are codons

Answer 13

combinations of 3 nucleotides in a row that dictate the amino acid. FIrst is Methionine

Question 14

Can stop codons encode

Answer 14

yes, there is lots of exceptions when stop codons action code, like in archea

Question 15

What is wobble base pairing

Answer 15

the third letter of the code doesn’t matter sometimes

Question 16

WHat structure do amino acids need to be in for ribosomes to incorporate them?

Answer 16

L amino structure, not D enantiomers

Question 18

How do we measure proteins

Answer 18

Dalton

Question 19

What leads to secondary structure?

Answer 19

interactions of amino acids with their neighbors, H bonds, disulfide bridges, ban der walls interactions, hydrophobic contacts

Question 20

WHat structures do we see in a secondary protein structure

Answer 20

alpha helicies, B pleated sheets (anti or paralel),

Question 21

Tertiary structures

Answer 21

R groups interact, final folding of pollypeptide, hydrophobic interactions, h bonding, charge pair interactions, van der walls

Question 22

Three main structures of tertiary structure

Answer 22

Globular proteins, FIbrous proteins, membrane proteins

Question 23

GLobular proteins

Answer 23

spherical, ex. lysozyme

Question 24

Fibrous proteins

Answer 24

long filamentous or rod-like structures, structural component of cell. like collagen or keratin, actin

Question 25

Membrane proteins

Answer 25

hydrophilic and phobic regions. ex. G protein-coupled receptor

Question 26

Quaternary structure

Answer 26

multiple polypeptides coming together. Functional proteins. can all be the same or different peptides

Question 27

What are dimers?

Answer 27

2 polypeptides, homodimers or heterodimers

Question 28

Multimers

Answer 28

multiple polypeptides like antibodies and hemoglobin

Question 29

What are macromolecular assemblages

Answer 29

molecular machines, proteins working together. For DNA rep, repair, recom, transcrip,

Question 30

WHat is a domain

Answer 30

functional importants, they do something and have unique functions

Question 31

What is a motif

Answer 31

chain like bio structure made up of conectivity between secondary structural elements, supersecondary structurem

Question 32

What are some Post-translational modifications

Answer 32

things can be added to them, they can be linked to other things, PHOSPHORYLATION of amino acid side chains

Question 33

Examples of proteins being joined covalently or non-covalently

Answer 33

lipoproteins, glycoproteins, metalloproteins

Question 34

What performs phosphorylation

Answer 34

kinases, they are specific to what they phosphorylate

Question 35

WHat allow proteins to fold correctly

Answer 35

molecular chaperones,

Question 36

are molecular chaperones doing work?

Answer 36

yes, need ATP, they also get rid of misfolded proteins

Question 37

what's another name for molecular chaperones

Answer 37

heat-shock proteins, aid in distructrion of misfolded proteins

Question 38

Where does folding take place

Answer 38

endoplasmic reticulum and then they're sent to the golgi

Question 39

What is ubiquitin-proteasome system

Answer 39

ubiquitin targets misfolded proteins via ubiquitination to a Lys. the proteasomes finds it and degrads that protein.

Question 40

what is macroautophagy

Answer 40

lysosomes take care of the misfolded proteins

Question 41

What is the primary cause of transmissible spongiform encephalophathies

Answer 41

prions

Question 42

types of prion diseases

Answer 42

sporadic, inherited, infectious (mad cow)