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Bio 100 > Exam 1: Eukarotes, Prokaryotes, Proteins, Carbohydrates > Flashcards

Exam 1: Eukarotes, Prokaryotes, Proteins, Carbohydrates Flashcards

1
Q

Prokaryotic cell

A

No nucleus but has protein
Chromosome: DNA and protein, colorful appearance, chromo= color

Plasmid: circular piece of DNA (contains genes)

Cytoplasm: gel like within cell membrane

Flagellum: moves around, whip like motion, comes from word whip

Ribosome: compound of ribonucleic acid + proteins. Key role in protein synthesis.

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2
Q

Eukaryotic cell

A 
Has nucleus. 
Golgi apparatus. 
Endoplasmid reticulums. 
Lysosomes 
Centrioles
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3
Q

Compartmentalization

A

Cell membrane semi permeable

Advantage: separation of incompatable rxns and efficiency of chem rxns increases

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4
Q

Euchromatin

A

Loosely packed sections of chromosomes in nucleus

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5
Q

Heterochromatin

A

Densely packed sections of chromosomes in nucleus

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6
Q

Nucleolus

A

RNA + Proteins. Ribosomes made

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7
Q

Nuclear envelop

A

Double membrane. Studded with pore like openings. Part of nucleus and Endoplasmic reticulum

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8
Q

Nuclear lamina

A

Fibrous protein net in nucleus

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9
Q

Rough Endoplasmic reticulum

A

Endo = inside; reticulum= network

Has ribosomes on it protein synthesis

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10
Q

Lumen

A

Inside of any sac like area

In Endoplasmic reticulum and Golgi

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11
Q

Golgi apparatus

A

Named after Camillo Golgi

Involved in packaging + modifying newly made proteins

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12
Q

Smooth Endoplasmic reticulum

A

Associated with lipid processing

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13
Q

Lysosome

A

40 enzymes.

Specialized for breaking up a diff type of macromolecule

Interior is acidic Ph of 5

Digestion and recycling

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14
Q

Phagocytosis

A

Ingesting of cell or particle

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15
Q

Autophagy

A

Eat/break down damaged organelle

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16
Q

Pinocytosis

A

Cell drinking. Accumulating fluids by endocytosis.

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17
Q

Mitochondria

A

Power house. Double membrane.

Generates ATP

Have there own genes and DNA and chromosomes

Make their own ribosomes

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18
Q

Chloroplasts

A

In plant eukaryotic

Photo synthesis role

Double membrane: thylakoids= membrane bound flattened vesicles

Has own DNA

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19
Q

Peroxisome

A

Prevents dangerous chemicals and breaks it down to catalase enzymes

H2O2 is taken into pero. Then converted to H20

Processing of fatty acids

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20
Q

Differential centrifuge

A

Based on size. Size largest to smallest organelles

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21
Q

Density gradient centrifuge

A

Cell components deprecated by density. Into distinct bands

Top is lower density. Bottom is highest density

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22
Q

Actin

A

Strands in double helix

Cell shape by preventing tension. Cell division in animals. Movement of organelles

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23
Q

Intermediate filaments

A

Keratin. Vitamentin. Lamin.
Thick cables

Cell shape by resisting tension

Anchor nucleus and other organelles

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24
Q

Microtubules

A

Hollow tubes: alpha and beta

Cell shape by resisting compression

Motility via flagella

Move chromosomes

Growth of plant cell walls

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25
Kinesin
Motor protein. Carries vesicles along motortubular
26
Cell Wall
In plants Protection and structural support
27
Vacuole
In plants Storage depots. Fluid filled. Looks vacant. Take up to 80% of space.
28
Central dogma
DNA codes for mRNA, codes protein.
29
Transcription
Production of mRNA
30
Translation
Synthesis of protein from mRNA
31
How protein secreted from cell
1. Enters ER while being synthesized by ribosome 2. Protein exits ER travels to cis face of Golgi 3. Enters Golgi and moves through cistermae 4. Exits Golgi at trans face and moves to plasma membrane 5. Protein is secreted
32
Pulse chase exp.
Radioactive substance add then wash out after a few seconds. Then u wait and see where proteins are
33
Exocytosis
Vesicles filled with proteins fuse with plasma membrane. Putting protein on outside of cell.
34
Hemoglobin
Quaternary structures 4 globin subunits each has 1 heme group which binds to oxygen
35
Monomers
Individual amino acids
36
Polymer
Strung together amino acids
37
Ionized form of amino acid
Amino acid is base Carboxyl group is acid Ph of 7 amino acids are in this form
38
Creation of protein
Formation of peptide bonds between amino acids. The carboxyl end interacts with amino me of another amino acid.
39
Condensation reaction
Dehydration of reaction, water out monomer in.
40
Hydrolysis
Degradation of proteins Water in monomer out
41
Primary structure of protein
Order and connection of amino acids Amino acids joined by peptide bonds N terminus to C terminus First amino acid linked to N terminus
42
Hydrophobic
Non polar side groups
43
Hydrophilic
Charged or polar side groups
44
Change in PH
Change shape and function effects protons bond
45
Secondary structures
Hydrogen bonds between peptide chains. Carboxyl end to amino end. Alpha helix. Beta pleated sheet.
46
Which amino acids have increased helix shape
Methioninen, Alaine, leucine, glutamate, lysine
47
Tertiary structures
Hydrogen bonds with side chain and carboxyl Hydrogen bond with 2 side chains Hydrophobic interactions Disulfide bonds Ionic bonds
48
Quarternary
Different protein subunits get together to form a larger protein Function of protein relys on subunits
49
Competitive inhibition
Blocks active site. Regulatory molecule bonds to enzymes, the substrate can't bind. If increased regulatory molecules the regulatory mol will bind
50
Allosteric regulation
Regulatory molecule bonds somewhere other than the active site Induces a shape change that makes active site either available or unavailable to substrate If increased regulatory molecules substrate still bind
51
Monosaccharides
Monomers that polymerize to form polysaccharides
52
Glucose VS galactose
Different configurations of hydroxyl groups Carb and sugar
53
Aldose
Carboxyl group on end of carbon chain Carb and sugar
54
Ketose
Carboxyl group in middle of carbon chain Carb and sugar
55
Glucose ring forms
Alpha glucose: hydroxyl group down Beta glucose: hydroxyl group up
56
Maltose
Polymerization reaction between two alpha glucose Is a disaccharide Alpha 1,4-glycosidic linkage and water
57
Starch
Two alpha glucose Alpha 1,4-glycosidic linkage Energy source for plants
58
Amylose
Unbranched starch helix 1,4 glycosidic linkage
59
Amylopectin
Branched starch helixes 1,6 glycosidic linkage every 30 Cs
60
Glycogen
2 alpha glucose Lots of 1,4 glycosidic linkage and 1,6 linkage every 10 Cs Energy storage in animals: muscles and liver Highly branched
61
Cellulose
4 beta glucose Beta 1,4 glycosidic linkage Most abundant carb gives ridgity to plants Parellel strands
62
Chitin
2 N acetal glucosamine Beta 1,4 glycosidic linkage Exoskeleton or insects Parellel strands
63
Peptidoglycen
1 N acetyl muramic acid and N acetyl glucosamine Beta 1,4 glycosidic linkage Amino acid chain forms peptide bond Parellel strands
64
Ribosomes
No membrane. Large/small subunits complex of RNA and proteins Functions protein synthesis
65
Cytoskeleton
Structural support Movement of materials In some species movement of whole cell
66
Non polar amino acids
Have C and H side groups Glycine. Alaine. Valine. Leucine. Isoleucine. Metholine. Pheny-lalaline. Tryptophan. Proline.
67
Polar amino acids
OHs or NH2 and double bond O Serine. Therloline. Cysteine. Tryosine. Asparargine. Glutamine.
68
Acidic amino acids
Double bonded O to CH2 Aspertate. Glutamate.
69
Basic amino acids.
CH and NH Lysine. Arginine. Histidine.

Bio 100 (6 decks)

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