Exam 1: Eukarotes, Prokaryotes, Proteins, Carbohydrates Flashcards

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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
Q

Kinesin

A

Motor protein. Carries vesicles along motortubular

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26
Q

Cell Wall

A

In plants

Protection and structural support

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27
Q

Vacuole

A

In plants

Storage depots. Fluid filled.

Looks vacant. Take up to 80% of space.

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28
Q

Central dogma

A

DNA codes for mRNA, codes protein.

29
Q

Transcription

A

Production of mRNA

30
Q

Translation

A

Synthesis of protein from mRNA

31
Q

How protein secreted from cell

A
  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
Q

Pulse chase exp.

A

Radioactive substance add then wash out after a few seconds. Then u wait and see where proteins are

33
Q

Exocytosis

A

Vesicles filled with proteins fuse with plasma membrane. Putting protein on outside of cell.

34
Q

Hemoglobin

A

Quaternary structures 4 globin subunits each has 1 heme group which binds to oxygen

35
Q

Monomers

A

Individual amino acids

36
Q

Polymer

A

Strung together amino acids

37
Q

Ionized form of amino acid

A

Amino acid is base
Carboxyl group is acid

Ph of 7 amino acids are in this form

38
Q

Creation of protein

A

Formation of peptide bonds between amino acids. The carboxyl end interacts with amino me of another amino acid.

39
Q

Condensation reaction

A

Dehydration of reaction, water out monomer in.

40
Q

Hydrolysis

A

Degradation of proteins

Water in monomer out

41
Q

Primary structure of protein

A

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
Q

Hydrophobic

A

Non polar side groups

43
Q

Hydrophilic

A

Charged or polar side groups

44
Q

Change in PH

A

Change shape and function effects protons bond

45
Q

Secondary structures

A

Hydrogen bonds between peptide chains. Carboxyl end to amino end. Alpha helix. Beta pleated sheet.

46
Q

Which amino acids have increased helix shape

A

Methioninen, Alaine, leucine, glutamate, lysine

47
Q

Tertiary structures

A

Hydrogen bonds with side chain and carboxyl

Hydrogen bond with 2 side chains

Hydrophobic interactions

Disulfide bonds

Ionic bonds

48
Q

Quarternary

A

Different protein subunits get together to form a larger protein

Function of protein relys on subunits

49
Q

Competitive inhibition

A

Blocks active site. Regulatory molecule bonds to enzymes, the substrate can’t bind.

If increased regulatory molecules the regulatory mol will bind

50
Q

Allosteric regulation

A

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
Q

Monosaccharides

A

Monomers that polymerize to form polysaccharides

52
Q

Glucose VS galactose

A

Different configurations of hydroxyl groups

Carb and sugar

53
Q

Aldose

A

Carboxyl group on end of carbon chain

Carb and sugar

54
Q

Ketose

A

Carboxyl group in middle of carbon chain

Carb and sugar

55
Q

Glucose ring forms

A

Alpha glucose: hydroxyl group down

Beta glucose: hydroxyl group up

56
Q

Maltose

A

Polymerization reaction between two alpha glucose

Is a disaccharide

Alpha 1,4-glycosidic linkage and water

57
Q

Starch

A

Two alpha glucose

Alpha 1,4-glycosidic linkage

Energy source for plants

58
Q

Amylose

A

Unbranched starch helix

1,4 glycosidic linkage

59
Q

Amylopectin

A

Branched starch helixes

1,6 glycosidic linkage every 30 Cs

60
Q

Glycogen

A

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
Q

Cellulose

A

4 beta glucose

Beta 1,4 glycosidic linkage

Most abundant carb gives ridgity to plants

Parellel strands

62
Q

Chitin

A

2 N acetal glucosamine

Beta 1,4 glycosidic linkage

Exoskeleton or insects

Parellel strands

63
Q

Peptidoglycen

A

1 N acetyl muramic acid and N acetyl glucosamine

Beta 1,4 glycosidic linkage

Amino acid chain forms peptide bond

Parellel strands

64
Q

Ribosomes

A

No membrane. Large/small subunits complex of RNA and proteins

Functions protein synthesis

65
Q

Cytoskeleton

A

Structural support
Movement of materials
In some species movement of whole cell

66
Q

Non polar amino acids

A

Have C and H side groups

Glycine. Alaine. Valine. Leucine. Isoleucine. Metholine. Pheny-lalaline. Tryptophan. Proline.

67
Q

Polar amino acids

A

OHs or NH2 and double bond O

Serine. Therloline. Cysteine. Tryosine. Asparargine. Glutamine.

68
Q

Acidic amino acids

A

Double bonded O to CH2

Aspertate. Glutamate.

69
Q

Basic amino acids.

A

CH and NH

Lysine. Arginine. Histidine.