Biochemistry Flashcards

(108 cards)

1
Q

Acid

A
  • H+ ions > OH-
  • Proton donor, e- acceptor
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2
Q

Base

A
  • OH- ions > H+ ions
  • Proton acceptor, e- donor
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3
Q

Adhesion

A

H2O molecules are attracted to other things bc of polarity

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4
Q

Cohesion

A

H2O molecules stick to each other

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5
Q

Surface tension

A

H bonds stick together stronger on the surface

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6
Q

Capillary Action

A

Ability to move H2O upwards against gravity through small openings

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7
Q

Intramolecular

A

Bonds within same molecule

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8
Q

Intermolecular

A

Bonds btwn diff molecules

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9
Q

Disulfide Bridge

A

Single covalent bond btwn 2 molecules w/sulfur

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10
Q

Isomer

A
  • Compounds w/same formula but different shape & properties
  • Structural - diff structure
  • Geometric - diff spatial arrangement
  • Enantiomer - mirroir images
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11
Q

Functional Groups

A

Characteristic grps attached to skeletons of organic molecules

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12
Q

Organic & Inorganic

A
  • Molecules w/C = organic
  • Molecules w/o C = inoganic (generally)
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13
Q

Hydrocarbons

A

Organic molecules w/only C & H2

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14
Q

Hydroxyl

A
  • OH
  • In dehydration reaction
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15
Q

Carbonyl

A
  • Aldehyde (double bonded O2 + H) (COH)
  • Ketone (just doubled bonded O2) (CO)
  • On sugar molecules
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16
Q

Carboxyl

A
  • Double bonded O + OH (CO2H)
  • Acidic behaviours, amino acids
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17
Q

Amine

A
  • NH2
  • Basic behaviours, amino acids
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18
Q

Phosphate

A
  • PO4 (can be w/OH instead of just O)
  • Acidic behaviour, ATP reactions
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19
Q

Sylfhydryl

A
  • SH
  • Disulfide bridges for protein folding
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20
Q

Methyl

A
  • CH3
  • Hydrophobic, less reactive
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21
Q

Macromolecule

A

Large molecule covalently bonded to repeating units of smaller molecules

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22
Q

Dehydration Synthesis/Condensation

A
  • Build macromolecules
  • Anabolic
  • H + OH releases
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23
Q

Hydrolysis

A
  • Breaks apart
  • Catabolic
  • H2O is split into H + OH, added to molecules
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24
Q

Carbohydrates

A

Family of orgo molecules of C, H2, O2

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25
Simple Carbohydrates
Sugar
26
Common Carbohydrate
- Glucose (C6H12O6) - Fructose - Galactose - Pentose - Hexose (6)
27
Monosaccharides
- Single sugar molecules - Fuelling cellular metabolism
28
Alpha Glucose
H above OH
29
Beta Glucose
H below OH
30
Disaccharides
- 2 monosaccharides joined w/glycosidic linkage - nrg sources - depends on the monomers
31
Alpha Glycosidic Linkages
H on same side
32
Beta Glycosidic Linkage
H on opposite side
33
Polysaccharides
Long chain of monosaccharides
34
Cellulose
B glucose polymer held by 1-4 glycosidic bonds
35
Microfibrils
- parallel chains of cellulose - cell wall structure - fibre
36
Starch
- A glucose w/amylose + amylopectin (1-4 & 1-6) - nrg storage for plants - easily hydrolyzed
37
Glycogen
- A glucose molecules w/1-6 & 1-4 links - nrg storage for animal - hydrolyzed to release glucose
38
Chitin
- modified polysaccharide of b glucose - has nitrogen instead of OH - cell walls of fungi
39
Lipids
- Like carbs but smaller proportion of O2 - Simple (fats, oils) - Phospholipids - Steroids
40
Role of Lipid
- 2x nrg - Waterproofing - Cell membrane - Absorbs shock - metabolic H2O - insulation
41
Types of Fatty Acids
- Monoglyceride (1 fatty acid) - Diglycerides - Triglycerides (most common)
42
Triglycerides
- Glycerol + 3 fatty acids - When glycerol bonds, ester bond is created & H2O
43
Saturated Fatty Acids
- Max # of H atoms, no double bond - Staight chains - Solid at room temp
44
Unsaturated Fatty Acids
- Double bonded C - Liquid at room temp
45
Cis Fatty Acids
H atoms are on the sane side of double bonded C
46
Trans Fatty Acids
- Opposite sides - Lies straight, not natural
47
Phospholipids
- glycerol + 2 fatty acids + PO4 - PO4 is hydrophillic & polar - Fatty acid is nonpolar & hydrophobic
48
Steroids
- 3 6 carbon atoms rings + 1 5 carbon ring - attaches onto a chain that changes
49
Sucrose
A glucose + B fructose
50
Maltose
A glucose + A glucose
51
Lactose
B glucose + B galactose
52
Phospholipid Bilayer
- Fatty acid tail + phosphate head - Naturally forms w/hydrophobic ends facing each other
53
Proteins Functions
- Structural - Enzymes - Cell receptors - Regulates/maintains - Transport molecules - Defense
54
Protein Elements
- Amino acid polymers folded a certain way - Sequence = shape
55
Amino Acid
- C in the middle + R (=diff functional grps + hydrocarbon chain) - Amine - Carboxyl
56
Complete Proteins
Proteins w/all essential amino acids
57
Polypeptides form
- Built in 1 dir - OH lost on carboxyl, & H lost on amine
58
Terminus for Amino Acids
- N terminus: end w/amino group - C terminus: carboxyl group
59
Primary Level
Amino acids order
60
Secondary Level
- Folds from H bonds - A helices (coil) - B pleated sheets (ribbon)
61
Tertiary Level
- Interaction (stabilizers) btwn distant amino acids - Hydrophobic aminos makes bubble - H + ionic bonds btwn R grps - Disulfide bridges
62
Quaternary
2+ tertiary polypeptides come together to make protein
63
Denaturation
- alteration of protein's shape - Caused by pH, salinity, hot temps, chems - Some can go back if polypeptide is ok
64
DNA
- Deoxyribonucleic acid - Deoxyribose sugar - A,C,G,T
65
RNA
- Ribonucleic acid - Ribose sugar - A,C,G,U
66
Nucleic Acid
polymers made of nucleotides
67
Nucleotides
- phosphate - sugar (2 types) - base (5 types)
68
Nucleotide Nitrogenous Bases
- Adenine - Guanine - Cytosine - Thymine - Uracil
69
Purines
- PuGA-2 - Double ring - Adenine & Guanine - Pairs w/pyrimidines
70
Pyrimindines
- PyCUT-1 - Single ring - Cytosine, thymine, uracil
71
Formation of Nucleic Acid
polynucleotide covalently link btwn phosphate & sugar of the other
72
RNA Function
- Transfer RNA - Messenger RNA - Ribosomal RNA
73
Adenine bonds with
Thymine
74
Guanine bonds with
Cytosine
75
DNA Backbone
atlernating PO4 + sugar (hydrophillic) molecules of the DNA
76
DNA strands
- Run antiparallel - 5' is across the 3' - PO4 on 5' carbon - OH on 3' carbon
77
DNA Function
- Info - Stable molecule - Replicate easy but allows mutations
78
Fatty Acids
Long hydrocarbon + carboxyl
79
Glycerol
Alcohol w/3 C, each bonded to OH
80
Cholesterol
Sterol lipid
81
Glycosidic Linkage
Bond btwn two monosaccharides
82
Ester Links
Bonds fatty acids & glycerol
83
Dipeptide Link
Two amino acids linked w/a peptide bond
84
Peptide Bond
Covalent bond btwn C and N atoms of adjacent amino acids
85
Phosphodiester Link
Bond btwn PO4 of one nucleotide w/other nucleotide's sugar
86
Different Types of Links
- Carbs: glycosidic links - Lipids: ester links - Proteins: peptide links - Nucleic Acids: phosphodiester bond
87
Concentration gradient
diff in C from inside to outside
88
Passive Transport & Types
- movement from high to low, no nrg - simple diffusion - facilitated diffusion - osmosis
89
Simple diffusion
happens directly through cell membrane
90
Facilitated Diffusion
high to low C w/help of proteins in membrane
91
Types of proteins for Facilitated Diffusion
- Channel proteins: allows ions/small polar things to pass through (tunnels) - Carrier proteins: binds to specific molecules, changes shape (gates)
92
Osmosis
movement of H2O from low to high C across membrane
93
Hypertonic Solution
solution w/higher C
94
Hypotonic Solution
solution w/lower C
95
Extracellular Fluid
fluids/things around cell
96
Factors that affect the Phospolipid bilayer
- Temp - Types of fat (sat or unsat) - Fatty acid tail length
97
Integral & Peripheral Protein
- Integral: embedded - Peripheral: outside - Helps transports, bind, precepts
98
Glycoprotein & Glycolipid
- Glycoprotein = carb + protein - Glycolipid = carb + lipid
99
Factors that affect diffusion
- molecule size - polarity - temp - pressure
100
Isotonic
same solute & H2O C
101
Exocytosis
vesicles w/things are released & fuse w/cell membrane
102
Endocytosis
cell engulfs w/cell membrane to form vesicle
103
Types of Endocytosis
- Phagocytosis: engulfs whole - Pinocytosis: sucks it in, then surrounds - Receptor-mediated: receptors bind w/molecules then takes it in
104
Active transport
- low to high - needs atp
105
ATP
- base + sugar + 3 PO4 - nrg releases when PO4 is taken off (adenosine diphosphate)
106
Ion pump
Actively transports ions against concentration gradient
107
Primary Active Transport
uses ATP directly to move against by taking a PO4 from ATP & attaching to protein channel
108
Secondary Active Transport
uses electrochemical gradient built from prior active transport to move molecules