Ch 4

Question 1

Satellite RNA

Answer 1

ssRNA genome, needs another virus to replicate, ex hepatitis

Question 2

Virusoids

Answer 2

SsRNA genome, like viroids with capsid, need helper virus to replicate

Question 3

Proteins are made of

Answer 3

Amino acids, chain like polymer

Question 4

Four types of Amino acid

Answer 4

Acidic, basic, polar, and non polar

Question 5

Amino acids are bound by

Answer 5

Peptide bonds with a condensation reaction

Question 6

Residues

Answer 6

When amino acids are joined in a series ofpeptide bonds

Question 7

Peptide

Answer 7

Short chain of amino acids

Question 8

Coding/sense strand

Answer 8

Same as RNA, but U is used instead of T

Question 9

Antisense strand/ template strand is read

Answer 9

3’to 5’, read by RNA polymerase

Question 10

How many codons possible

Answer 10

64

Question 11

Synonymous codon

Answer 11

Two diff codons with the same amino acid associated

Question 12

Degenerate code

Answer 12

Some codons can mean the same thing

Question 13

One tRNA can recognize more than one codon with

Answer 13

Wobble

Question 14

Wobble

Answer 14

tRNA specific to a particular amino acid recognize multiple codon triplets that differ only in the third letter

Question 15

Modified bases on tRNA anti codon allow for

Answer 15

Recognition of more codons by one tRNA

Question 16

What amino acid isomer do living organism usually use

Answer 16

L-amino acids for protein making

Question 17

Dalton unit

Answer 17

Molecular weight of protein, average amino 110 da

Question 18

Protein primary structure

Answer 18

Amino acids

Question 19

Secondary structure

Answer 19

Amino acids reacting to fold, stabilized with hydrogen bonds

Question 20

Three protein secondary structures

Answer 20

A helix, b pleated sheet, unstructured turn

Question 21

A helix

Answer 21

Most common, helical structure stabilized with h bonds with aminos, proline prevents helix

Question 22

Beta pleated

Answer 22

Secondary common, h bonds between backbone, can be parallel or antiparrallel

Question 23

Unstructured turns

Answer 23

Allow for helix and pleats to interact, short loops

Question 24

Tertiary structure of protien

Answer 24

3D shape of one polypeptide,
Stabilized with hydrophobic interactions, hydrogens bonds, van Dee walls, just non covalent stuff

Question 25

Disulfide bridges

Answer 25

Bridges between cysteines, main and strongest covalent bond with polypeptide

Question 26

Tertiary structure types

Answer 26

Globular, fibrous, membrane

Question 27

Globular proteins

Answer 27

Rough sphere, most common
Ex. Lysozyme

Question 28

Fibrous protiens

Answer 28

Rod like, structural components of cells and tissues,
Made of: coils, anti parallel pleated sheets, trip helical arrangement
Ex. Collagen, keratin

Question 29

Membrane protein

Answer 29

Interact with membrane, ex seven transmembrane helix structure, hydrophobic and hydrophilic parts

Question 30

Quaternary structure

Answer 30

Multiple polypeptide subunits, same non covalent stabilizers as tertiary structure

Question 31

Dimer

Answer 31

2 polypeptides

Question 32

Multimers

Answer 32

More than 2 polypeptides,
Ex. Hemoglobin

Question 33

Macro molecular assemblages

Answer 33

Hella polypeptides,
For: DNA replications, repair, recombination, and yea

Question 34

Intrinsically disordered protiens

Answer 34

Lack secondary and tertiary structure, fucked up
Ex. Amyloid beta and synuclein, linked with Alzheimer’s and stuff

Question 35

Domains (tertiary)

Answer 35

Larger proteins (20+ kDA), perform specific functions like DNA binding, can have patterns and shit, usually made with a continuous amino acid sequence

Question 36

Protiens functions as

Answer 36

Enzymes (catalysts),

Question 37

Post translational modifications

Answer 37

Amino acid mods, add lipids, metals, and phosphorylation and others

Question 38

Kinases

Answer 38

Catalyze addition of phosphate group

Question 39

Phosphatase

Answer 39

Remove phosphates, less specific

Question 40

Two kinase types (euk)

Answer 40

Serine or Threonine side chains, tyrosine side chains
Need specific substrate

Question 41

Allosteric regulation

Answer 41

Change of shape to regulate protien activity, can increase or decrease activity

Question 42

Heat shock protiens

Answer 42

molecular chaperones, promote proteins folding and aid in destruction of misfolded proteins

Question 43

HSP 70 and HSP 40

Answer 43

Common heat shock protiens

Question 44

Endoplasmic reticulum “quality control”

Answer 44

protiens are sent to ER to fold from Golgi apparatus (chaperones here), missfolded are then taken care of

Question 45

Ubiquitin proteasome system

Answer 45

Protein degradation in eukaryotes

Question 46

Ubiquitin

Answer 46

Tags a protein to an amino acid

Question 47

After Ubiquitin tags amino acid

Answer 47

A chain of Ubiquitin forms, Proteasome targets the protiens, Ubiquitin is released, protiens destroyed

Question 48

Chaperones mediated autophagy

Answer 48

Protein degradation, HSP 70 targets misfolded protiens to lysosome

Question 49

Macroautophagy

Answer 49

Proteins degradation process, atuopphagosome formed

Question 50

Amyloid fibrils

Answer 50

Normally soluble proteins turn insoluble and accumulate

Question 51

Human protein misfolding diseases

Answer 51

Alzheimer’s, Parkinson’s, huntingtons, type II diabetes, creuzfeldt Jakob

Question 52

codon bias

Answer 52

Multiple ways to construct a set of tRNAs able to recognize all codons
ex. wobble baes pairing and modded bases

Question 53

allosteric regulation induced by

Answer 53

ligands

Question 54

molecular chaperones are independent of

Answer 54

ATP

Question 55

proteasome

Answer 55

degrades ubiquitin tagged protien