Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Cell Biology > Proteins > Flashcards

Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

Proteins

A

Biopolymers of amino acids joined by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Amino acids

A

molecules containing an amine group, carboxylic acid group, and a side chain that varies

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

proteinogenic

A

natural amino acids; 22 amino acids that are used in polypeptides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

non-proteinogenic

A

amino acids that are not used for making proteins or amino acids that are produced indirectly (e.g. hydroxyproline)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Unusual amino acids

A

expansions of the genetic code

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

pyrrolysine and selenocysteine are only made when what is present?

A

selenium

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Amber

A

UAG stop codon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Opal

A

UGA stop codon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

making a prokaryote timeline

A

minutes to hours

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

making a eukaryote timeline (human cells)

A

hours to days

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

why is translation in eukaryotes slower?

A

more complex, extra time needed for post-translational modification

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

why are prokaryotes faster?

A

transcription and translation are coupled

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

membrane bound ribosomes

A

On rough ER, proteins targeted for release

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

free ribosomes

A

in cytosol, proteins used within the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Ribosomes

A

2 subunits and are named according to rate of sedimentation (Svedberg is 10^-13 seconds)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

polysomes (polyribosomes)

A

translational parallel processing. More than 1 ribosome can be attached to single mRNA at a time

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

polysomes were originally called what?

A

ergosomes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Tetracyclin

A

antibiotic compounds isolated from dirt from graveyards; developed into aureomycin (which is a tetracycline). Tetracyclines bind reversible to the 30s subunit and prevents the binding of aminoacyl-t-RNA to the mRNA complex, PREVENTING BACTERIA FROM TRANSLATING NEW PROTEINS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

primary

A

sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

secondary

A

folding and coiling

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

tertiary

A

interactions between side chains (R groups)

22
Q

quaternary

A

interactions between polypeptides

23
Q

N-terminus (amide)

A

targeting, survival. (First AA determines half life, post-translationally modified for further processing)

24
Q

N end rule

A

identity of N termal AA determines how long the peptide can last before it degrades

25
Q

C-terminus (carboxyl)

A

retention, sorting. KDEL most common sequence for ER retentions; post-translationally modified for further processing. Contains signals for later protein sorting.

26
Q

KDEL

A

most common amino acid sequence

27
Q

Polar Side Chains

A

AA side chains tend to gather on outside of the protein; can interact with water

28
Q

Non-polar side chains

A

AA side chains are buried on the inside of tight packed structure

29
Q

Secondary structure shapes are formed by what?

A

hydrogen bonds

30
Q

tertiary structure

A

3D protein structure, created by interaction between the side chains. Mostly determined by the primary structure

31
Q

dimer

A

two identical peptide chains bind together

32
Q

dimer

A

two identical peptide chains bind together

33
Q

heterodimer

A

two different peptide chains bind together

34
Q

N-linked glycosylation

A

sugar group is added covalently to the N terminus (it becomes a glycoprotein)

35
Q

Glycosylation occurs in what?

A

all eukaryotes but not prokaryotes

36
Q

If proteins accumulate in CYTOSOL

A

chaperone proteins are activated or produced to help re-fold misfiled proteins

37
Q

Unfolded protein response (UPR)

A

occurs when proteins occur in the ENDOPLASMIC RETICULUM

38
Q

what degrades misfiled proteins?

A

enzymes

39
Q

what refold misfiled proteins?

A

chaperones

40
Q

apoptosis

A

cell gives up/ death by cell

41
Q

Prions

A

Creutzfeldt-Jacob Disease/Mad Cow disease/bovine spongiform encephalothapy

42
Q

Prions

A

misshapen PrP protein capable of changing the shape of other proteins

43
Q

Sequencing: Edman degradation

A

Break off N-terminal AA one by one and run on gen to identify (labour intensive, similar to Sanger sequencing)

44
Q

Mass spectroscopy

A

measure mass to charge ration.

45
Q

BLAST

A

search tool you can put sequence into to see what the corresponding sequence/ gene is for (Basic Logical Alignment Search Tool

46
Q

Southern Blots

A

DNA

47
Q

Northern Blots

A

RNA

48
Q

Immunoblotthing: Western Blotting

A

rapid and sensitive assay for the detection and characterization of proteins that works by exploiting the specificity inherent in antigen-antibody recognition

48
Q

Immunoblotthing: Western Blotting

A

rapid and sensitive assay for the detection and characterization of proteins that works by exploiting the specificity inherent in antigen-antibody recognition

49
Q

Immunohistochemistry

A

using antibodies to specific proteins to identify their presence and location in tissue samples. let anatomy decide location.

50
Q

ELISA (Enzyme Linked ImmunoSorbent Assay)

A

detects presence of proteins in a sample. Inverse of western. (Antibody to substrate first, then add sample to see if it sticks to antibody)

Cell Biology (5 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions