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Molecular Genetics > Ch 4 > Flashcards

Ch 4 Flashcards

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Biology 101 flashcards
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
Q

Disulfide bridges

A

Bridges between cysteines, main and strongest covalent bond with polypeptide

26
Q

Tertiary structure types

A

Globular, fibrous, membrane

27
Q

Globular proteins

A

Rough sphere, most common
Ex. Lysozyme

28
Q

Fibrous protiens

A

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

29
Q

Membrane protein

A

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

30
Q

Quaternary structure

A

Multiple polypeptide subunits, same non covalent stabilizers as tertiary structure

31
Q

Dimer

A

2 polypeptides

32
Q

Multimers

A

More than 2 polypeptides,
Ex. Hemoglobin

33
Q

Macro molecular assemblages

A

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

34
Q

Intrinsically disordered protiens

A

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

35
Q

Domains (tertiary)

A

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

36
Q

Protiens functions as

A

Enzymes (catalysts),

37
Q

Post translational modifications

A

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

38
Q

Kinases

A

Catalyze addition of phosphate group

39
Q

Phosphatase

A

Remove phosphates, less specific

40
Q

Two kinase types (euk)

A

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

41
Q

Allosteric regulation

A

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

42
Q

Heat shock protiens

A

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

43
Q

HSP 70 and HSP 40

A

Common heat shock protiens

44
Q

Endoplasmic reticulum “quality control”

A

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

45
Q

Ubiquitin proteasome system

A

Protein degradation in eukaryotes

46
Q

Ubiquitin

A

Tags a protein to an amino acid

47
Q

After Ubiquitin tags amino acid

A

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

48
Q

Chaperones mediated autophagy

A

Protein degradation, HSP 70 targets misfolded protiens to lysosome

49
Q

Macroautophagy

A

Proteins degradation process, atuopphagosome formed

50
Q

Amyloid fibrils

A

Normally soluble proteins turn insoluble and accumulate

51
Q

Human protein misfolding diseases

A

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

52
Q

codon bias

A

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

53
Q

allosteric regulation induced by

A

ligands

54
Q

molecular chaperones are independent of

A

ATP

55
Q

proteasome

A

degrades ubiquitin tagged protien

Molecular Genetics (13 decks)

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