Ch 4 Flashcards

(55 cards)

1
Q

Satellite RNA

A

ssRNA genome, needs another virus to replicate, ex hepatitis

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2
Q

Virusoids

A

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

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3
Q

Proteins are made of

A

Amino acids, chain like polymer

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4
Q

Four types of Amino acid

A

Acidic, basic, polar, and non polar

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5
Q

Amino acids are bound by

A

Peptide bonds with a condensation reaction

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6
Q

Residues

A

When amino acids are joined in a series ofpeptide bonds

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7
Q

Peptide

A

Short chain of amino acids

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8
Q

Coding/sense strand

A

Same as RNA, but U is used instead of T

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9
Q

Antisense strand/ template strand is read

A

3’to 5’, read by RNA polymerase

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10
Q

How many codons possible

A

64

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11
Q

Synonymous codon

A

Two diff codons with the same amino acid associated

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12
Q

Degenerate code

A

Some codons can mean the same thing

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13
Q

One tRNA can recognize more than one codon with

A

Wobble

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14
Q

Wobble

A

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

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15
Q

Modified bases on tRNA anti codon allow for

A

Recognition of more codons by one tRNA

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16
Q

What amino acid isomer do living organism usually use

A

L-amino acids for protein making

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17
Q

Dalton unit

A

Molecular weight of protein, average amino 110 da

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18
Q

Protein primary structure

A

Amino acids

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19
Q

Secondary structure

A

Amino acids reacting to fold, stabilized with hydrogen bonds

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20
Q

Three protein secondary structures

A

A helix, b pleated sheet, unstructured turn

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21
Q

A helix

A

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

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22
Q

Beta pleated

A

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

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23
Q

Unstructured turns

A

Allow for helix and pleats to interact, short loops

24
Q

Tertiary structure of protien

A

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

25
Disulfide bridges
Bridges between cysteines, main and strongest covalent bond with polypeptide
26
Tertiary structure types
Globular, fibrous, membrane
27
Globular proteins
Rough sphere, most common Ex. Lysozyme
28
Fibrous protiens
Rod like, structural components of cells and tissues, Made of: coils, anti parallel pleated sheets, trip helical arrangement Ex. Collagen, keratin
29
Membrane protein
Interact with membrane, ex seven transmembrane helix structure, hydrophobic and hydrophilic parts
30
Quaternary structure
Multiple polypeptide subunits, same non covalent stabilizers as tertiary structure
31
Dimer
2 polypeptides
32
Multimers
More than 2 polypeptides, Ex. Hemoglobin
33
Macro molecular assemblages
Hella polypeptides, For: DNA replications, repair, recombination, and yea
34
Intrinsically disordered protiens
Lack secondary and tertiary structure, fucked up Ex. Amyloid beta and synuclein, linked with Alzheimer’s and stuff
35
Domains (tertiary)
Larger proteins (20+ kDA), perform specific functions like DNA binding, can have patterns and shit, usually made with a continuous amino acid sequence
36
Protiens functions as
Enzymes (catalysts),
37
Post translational modifications
Amino acid mods, add lipids, metals, and phosphorylation and others
38
Kinases
Catalyze addition of phosphate group
39
Phosphatase
Remove phosphates, less specific
40
Two kinase types (euk)
Serine or Threonine side chains, tyrosine side chains Need specific substrate
41
Allosteric regulation
Change of shape to regulate protien activity, can increase or decrease activity
42
Heat shock protiens
molecular chaperones, promote proteins folding and aid in destruction of misfolded proteins
43
HSP 70 and HSP 40
Common heat shock protiens
44
Endoplasmic reticulum “quality control”
protiens are sent to ER to fold from Golgi apparatus (chaperones here), missfolded are then taken care of
45
Ubiquitin proteasome system
Protein degradation in eukaryotes
46
Ubiquitin
Tags a protein to an amino acid
47
After Ubiquitin tags amino acid
A chain of Ubiquitin forms, Proteasome targets the protiens, Ubiquitin is released, protiens destroyed
48
Chaperones mediated autophagy
Protein degradation, HSP 70 targets misfolded protiens to lysosome
49
Macroautophagy
Proteins degradation process, atuopphagosome formed
50
Amyloid fibrils
Normally soluble proteins turn insoluble and accumulate
51
Human protein misfolding diseases
Alzheimer’s, Parkinson’s, huntingtons, type II diabetes, creuzfeldt Jakob
52
codon bias
Multiple ways to construct a set of tRNAs able to recognize all codons ex. wobble baes pairing and modded bases
53
allosteric regulation induced by
ligands
54
molecular chaperones are independent of
ATP
55
proteasome
degrades ubiquitin tagged protien