Midterm 2 Flashcards

1
Q

Condensation / Dehydration reactions

A

Newly formed peptide bond results in loss of a water molecule and polymerizes monomers

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

Hydrolysis

A

Breaks polymers apart by adding a water molecule

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

Peptide bond

A

The C-N covalent bond that results from condensation reaction of one carboxyl group and one amino group, unusually stable

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

Protein primary structure

A

Unique sequence of amino acids in a protein, fundamental to function and directs the folding- still intact when denatured

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

Protein secondary structure

A

Created by hydrogen bonding between components of the peptide bonded backbone (helices or sheets), link backbone components together

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

Protein tertiary structure

A

Overall shape of a polypeptide from interactions between r groups or r groups and backbone

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

Protein quaternary structure

A

The combination of multiple polypeptides in a protein structure, held together same way as in tertiary, not all proteins have this

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

Prions

A

Proteins folded infectious disease-causing agents, not necessarily different in amino acid components, just shape, cause disease called spongiform encephalopathies

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

Amino acid general structure

A

Amino functional group, Carboxyl group, R group side chain, Hydrogen

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

Nonpolar side chain

A

Carbons and Hydrogens galore (don’t let Sulphur throw you)

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

Polar side chain

A

OH or O and H2N together

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

Acidic side chain

A

Negative charge, Carbon with oxygen

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

Basic side chain

A

Positive chain, NH3/2/1

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

Five tertiary side chain interactions

A

Hydrogen bonding, van der Waals forces, covalent, hydrophobic interactions, ionic bonds

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

Amino acid folding in solution spontaneous? Why?

A

Yes, van der Waals forces and hydrophobic interactions > entrophy

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

Protein functions

A

Catalyze, defence, structure, motor, transport, carry signal

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

Purines

A

Adenine, Guanine

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

Pyrimidines

A

Cytosine, Uracil, Thymine

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

Phosphodiester linkage

A

Forms between hydroxyl and phosphate group joins the 5’ carbon on one nucleotide to 3’ carbon of other, depending on if it contains ribose in sugar or deoxyribose determines identity

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

Nucleotide general

A

Phosphate group, five carbon structure, nitrogenous base

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

Complementary base pairs

A
In DNA, # of purines = # of pyrimidines 
#Ts = #As = #Cs = #Gs
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

RNA and DNA differences

A

RNA has ribose (with extra Hydroxyl, so more reactive) DNA has deoxyribose, also uracil vs. thymine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Five major types of RNA

A

Ribosomal
Messenger (carry info to manufacture proteins)
Transfer
Small nuclear: involved in processing messenger RNAs, getting them ready
Micro: important for regulating gene expression

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Glycosidic linkage

A

Covalent interaction formed by condensation reaction between two hydroxyl groups in monosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Starch
Stored for later use in plant cells, entirely alpha glucose monomers joined by glycosidic linkages, causes chain to coil into helix with branch points ever 1-30
26
Glycogen
Same storage purpose but in animals with liver and muscles and has it's branched link every 10 instead of every 30 subunits
27
Cellulose
Major component of plant cell wall, provide structural support because has beta monomers that form linear chain allowing for long parallel strands to make H bonds (close to starch but beta)
28
Chitin
Stiffins cell wall of fungi, similar to cellulose in its long tough sheets it forms but does it with N-acetylglucosamine instead, found as arthropod exoskeleton and fungi and algae
29
Peptidoglycan
Provides strength and firmness to bacteria cell walls, has amino acids linked to it that form peptide bonds with each other when they line up
30
Carb functions
Precursors for large molecules Provide fibrous structural materials (cellulose, chitin, and peptidoglycan, keep water out and few things can break down) Indicate cell identity: vary a lot to so capable of displaying info to other cells through structure (sperm and egg) Store chemical energy: can be sunlight
31
Glycosidic linkages
Covalent interaction formed by condensation reaction between 2 hydroxyl groups in monosaccharides alpha 1-4 goes down, beta 1-4 goes up
32
Amylase
Helps starch be glucose in glycogen it's phosphorylase that changes it
33
Fatty acid
Simple, lipid consisting of hydrocarbon chain bonded to hydroxyl group
34
Fats
Nonpolar molecules linked to the 3 carbon glycerol and containing three fatty acids, primary role is for energy storage
35
Ester linkage
Joins glycerol and fatty acids, not for forming a polymer macromolecule
36
Steroids
Family of lipids distinguished by bulky four ring structure
37
Amphipathic
Compounds that contain both hydrophilic and hydrophobic elements
38
Isotonic
Concentration inside and outside are equal
39
Facilitated diffusion
Passive transport of substance that otherwise would not cross the membrane readily
40
Permeability rules
- Small, nonpolar molecules move across bilayers quickly - Small but polar molecules cross these layers at an intermediate rate - Unsaturated hydrocarbon tails make less selective, weaker bilayers - Short tail also easier to cross - Adding cholesterol dramatically reduces permeability - Temperature effects too since phospholipids slow down at colder temperatures
41
Channels
Form pores so ions can move to low concentration areas or opposite charge areas, highly specialized, always passive transport
42
Carriers
Specialized membrane proteins that change shape during the transport process
43
Pumps
Active transport proteins, ATP binds to and changes its shape
44
Plasmids
Contain genes but physically independent of the cellular chromosome small circular and super coiled, used to help cell adapt to unusual circumstances
45
Ribosomes
Protein manufacturing centre (single cell can have 10,000) (not an organelle)
46
Flagella
Base is embedded in plasma membrane | Has long, helical filament that propels cell through water
47
Fimbriae
Needle-like projections that extend from the plasma membrane
48
Fimbriae
Needle-like projections that extend from the plasma membrane
49
Cystosol
Fluid portion between plasma membrane and organelles
50
Nuclear envelope
Double membrane enclosing nucleus
51
Nuclear lamina
Fibrous proteins that form lattice-like sheets to stiffen and maintain shape
52
Nucleolus
Place where RNA molecules found in ribosomes are manufactured and large and small ribosomal subunits are assembled
53
Rough endoplasmic reticulum
Ribosomes associated with rough ER synthesize proteins that will be inserted into the plasma membrane, secreted to cell exterior or shipped to an organelle
54
Smooth endoplasmic reticulum
Contains enzymes that catalyze reactions involving lipids
55
Lumen
Name for interior of any sac-like structure in a cell or body
56
Golgi apparatus
Cis side receives products from rough ER, trans side ships them to other organelles
57
Lysosomes
Recycling centres in animal cells
58
Endomembrane system
Produces, processes, and transports proteins and lipids via the ER, lysosomes, and Golgi apparatus
59
Vacuole
Serve role of lysosome for plant cells, but larger, is a storage depot that can be filled with pigment or noxious compounds
60
Mitochondria
Powerhouse of the cell
61
Stroma
Region outside thylakoids that contains enzymes that use this chemical energy to produce sugars
62
Nuclear pores
Connect inside of nucleus with cytosol going through inner and outer membranes, RNA goes out but not DNA Nucleotides and certain proteins enter
63
Nuclear localization signal
Found in nuclear pores, a sequence zipcode that marks proteins for transport through the nuclear pore complex Zipcode has it open so it can pass through
64
ER signal sequence
Sequence of amino acids that will move proteins into the ER lumen
65
Glycosylation
Addition of one or more carbohydrate group(s)
66
Early endosome
Transient organelle where endocytic vesicles drop off cargo, activity of proton pumps makes them acidic so releases cargo
67
Late endosome
Pre-lysosomal compartment where the acid hydrolases from the Golgi apparatus are dropped off
68
Autophagy
How damaged organelles' components are digested and recycled in the lysosome
69
Phagocytosis
Plasma membrane of cell surrounds small things, engulfs them, and takes them to the lysosome for digestion
70
Cytoplasmic streaming
Common in large cells, occurs along actin powered by myosin | Directed flow of organelles and cytosol in plant cells
71
Cell crawling
Groups of actin filaments grow creating bulges in plasma membrane to extend cell forward
72
Intermediate filament
Consist of different types of protein (unlike filament and microtubules), are not polar just purely structural Ex: Keratin
73
Nuclear lamins
Qualify as intermediate filament, they anchor chromosomes and help nuclear envelope break up and reassemble in cell division
74
Microtubules
Consist of an alpha tubulin and beta tubulin polypeptide that create large hollow tubes Grow faster at alpha + end
75
Microtubule organizing center
Origin of microtubules, they grow with their + end outward
76
Centrosome
Structure in microtubule organizing centre (MOC) of animal cells with 2 centrioles that are themselves bundles of microtubules
77
Prokaryotic organelles
Nucleoid, plasmids, and ribosomes but common to have extensive internal membrane for photosynthesis
78
Prokaryotic vs. Eukaryotic
- Eukaryotic chromosomes found inside a membrane bound compartment called nucleus - Eukaryotic cells are larger (messes up volume to SA ratio so they need organelles) - Eukaryotic cells contain extensive amounts of internal membrane - Eukaryotic cells feature particularly diverse and dynamic cytoskeleton
79
Pathway through endomembrane system
- Free ribosome uses ER signal to get it to ER, signal sequence then removed - From rough ER, transported in vesicles that bud off from ER - To Golgi: cisternae form on cid side of golgi and break away replaced by those behind it - To secretory vesicles out of cell: Need mannose-6-phosphate to be transferred to lysosome, like other signals, binds to trans-golgi, different signal for different place
80
G1 Checkpoint
- Size - Availability of nutrients (extra pertinent for single celled organisms) - Social signals (response to signalling molecules from other cells) - Damage to DNA (p53, a tumor suppressor, stops cycle until damage repaired, or causes apoptosis, programmed death)
81
Defects in cancer cells
- Proteins required for cell growth are active when they shouldn't be - Defects that prevent tumour suppressor genes from shutting down cell cycle
82
Catabolic pathways
Break down molecules for source of energy and carbon building blocks
83
Anabolic pathways
Those that use energy and carbon building blocks to synthesize molecules
84
Cofactors
Inorganic ions which reversibly interact with enzymes
85
Coenzymes
Organic molecules that reversibly interact with enzymes