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Physiology Exam #1 > Biomolecules and Protein Synthesis > Flashcards

Biomolecules and Protein Synthesis Flashcards

1
Q

Types of chemical bonding

A

ionic, covalent, hydrogen

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2
Q

Ionic bond (what it is, electronegativity, example)

A
  • Electron is transferred from one element to another
  • Electronegativity: one strong, one weak
  • between 2 ions with opposite charges
  • Ex: Nacl
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3
Q

Covalent bond (what it is, electronegativity, examples)

A
  • electrons are shared
  • electronegativity is relatively equal
    • non-polar: equal sharing ex: CH4
    • polar: unequal sharing ex: H2O
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4
Q

Hydrogen bond (what it is, examples)

A
  • opposite partial charges on adjacent molecules –> attraction
  • slight (+) charges (near H) and (-) charges (near O) –> attraction
    ex: water molecules binding to each other
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5
Q

Biomolecules (3 points)

A
  • molecules synthesized by cells
  • contain c-c covalent bonds
  • often form ring or chain structures
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6
Q

How do we make biomolecules?

A

Dehydration synthesis: forming covalent bonds by removal of H2O

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7
Q

How do we break biomolecules?

A

hydrolysis: breaking covalent bonds by the addition of water

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8
Q

Types of biomolecules

A

carbohydrates, lipids, proteins, nucleic acids

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9
Q

Carbohydrates (contain, properties, types)

A

Contain: C,H,O (C+H2O)
Properties: polar –> hydrophilic
Types: simples sugars, complex carbohydrates

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10
Q

Simple sugars (function, types, examples)

A

function: fast energy
Types:
-monosaccharide: one sugar (glucose, fructose)
-disaccharide: two sugars (sucrose, lactose)

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11
Q

Complex carbohydrates (function, type, examples)

A

Function: energy storage, structural support, component of cell membranes
types:
-polysaccharide: chain of sugars (starch, glycogen, cellulose, chitin)

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12
Q

Lipids (contain, properties, types)

A 
Contain: C,H,O
properties: non-polar --> hydrophobic
Types:
  -Triglycerides
  -Phospholipids
  -Eiconosids
  -Steroids
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13
Q

Triglycerides (structure, function, types)

A 
Structure: glycerol, 3 fatty acid chains
Function: energy storage, insulation, protection
Types: 
1. saturated
  -no double bonds
  -tightly packed
  -solid at room temperature
2. unsaturated
  -contains double bonds
  -loosely packed
  -liquid at room temperature
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14
Q

Phospholipids (structure, function)

A 
Structure:
  -glycerol
  -phosphate group (polar)
  -two fatty acid tails (non-polar)
Function: membrane structure
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15
Q

Eiconosids (structure, function, example)

A 
Structure:
  -ring structure
  -fatty acids
Function: cellular communication
Example: Prostaglandin (pain perception)
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16
Q

Sterols (structure, function, examples)

A 
Structure:
  -4 carbon rings with side chains
  -all derived from cholesterol
Function:
  -membrane fluidity
  -cellular communication
  -others
Examples:
  - cholesterol, testosterone, vitamin D
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17
Q

Proteins (contain, structure, function)

A 
Contain: C,H,O,N
Structure: chain of folded amino acids (polypeptide)
Function:
  -structural support
  -enzymatic activity
  -chemical messengers
  -receptors
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18
Q

Amino acid structure

A
  1. central carbon
  2. amino group: NH2
  3. carboxyl group: COOH
  4. R group: determines amino acid
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19
Q

Protein structural levels

A
  1. primary: sequence of amino acids (peptide bonds)
  2. secondary: structural motifs (H bonds)
    - Alpha-helix: spirals
    - Beta-pleaded sheets: pleads
  3. tertiary: large scale motifs formed by the interactions between R-groups (H-bonds, ionic bonds, disulfide bonds)
  4. quaternary: bonding with multiple polypeptide chains
20
Q

Nucleic acids (contain, properties, structure, function, types)

A 
Contain: C,H,O,N,p
Properties: polar --> hydrophilic
Structure: chain of nucleotides
Function:
  1. store genetic information (DNA)
  2. DNA expression (RNA)
Types: DNA, RNA
21
Q

Nucleotide (what is it made of)

A
  1. phosphate group
  2. Nitrogenous base
    - adenine, guanine, cytosine, thymine (DNA), uracil (RNA)
22
Q

DNA (structure, sugar, what binds to adenine)

A
  • double stranded helix
  • sugar: deoxyribose
  • thymine binds to adenine
23
Q

RNA (structure, sugar, what binds to adenine, types)

A
  • single stranded
  • sugar: ribose
  • uracil binds to adenine
  • types:
    • mRNA: messenger RNA, nucelus –> ribosome
    • tRNA: transfer RNA, important in protein synthesis
    • rRNA: ribosomal RNA, part of the ribosome
24
Q

Plasma Membrane

A
  • Structure: lipid bilayer with scattered proteins and cholesterol molecules
  • Function: maintains boundary of cell and integrity of cell structure: embedded proteins serve multiple functions
25
Q

Nucleus

A
  • Structure: Surrounded by double layered nuclear envelope

* Function: houses the DNA, which dictates cellular function in protein synthesis

26
Q

Nucleolus

A
  • Structure: Dark oval structure inside the nucleus

* Function: synthesis of ribosomal DNA

27
Q

Cytosol

A
  • Structure: gel-like fluid

* Function: cell metabolism; storage

28
Q

Rough Endoplasmic Reticulum

A
  • Structure: continuous with the nuclear envelope; flattened stacks dotted with ribosomes
  • Function: protein synthesis and post-translational processing
29
Q

Smooth Endoplasmic Reticulum

A
  • Structure: continuous with rough endoplasmic reticulum; tubular structure without ribosomes
  • Function: lipid synthesis and post-translational processing of proteins; transport of molecules from endoplasmic reticulum in Golgi apparatus, calcium storage
30
Q

Golgi Apparatus

A
  • Structure: series of flattened sacs near the endoplasmic reticulum
  • Function: post-translational processing; packaging and sorting of proteins
31
Q

Mitochondria

A
  • Structure: oval shaped with outer membrane and an inner membrane with folds called cristae that project into the matrix
  • Function: ATP synthesis
32
Q

Lysosomes

A
  • Structure: granular, saclike; scattered throughout cytoplasm
  • Function: breakdown of cellular and extracellular debris
33
Q

Peroxisomes

A
  • Structure: similar in appearance to lysosomes, but smaller

* Function: breakdown of toxic substances, including hydrogen peroxide

34
Q

Vaults

A
  • Structure: small, barrel-shaped

* Function: unknown; possibly transport of molecules between nucleus and cytoplasm

35
Q

Ribosomes

A
  • Structure: granular organelles composed of proteins and rRNA- located in cytosol or on surface of rough endoplasmic reticulum
  • Function: translation of mRNA to synthesize proteins
36
Q

Centrioles

A
  • Structure: two cylindrical bundles of protein filaments that are perpendicular to each other
  • Function: direction of mitotic spindle development during cell division
37
Q

Cytoskeleton

A
  • Structure: composed of protein filaments, including microfilaments, intermediate filaments, and microtubules
  • Function: Structural support of cell; movement and contraction
38
Q

DNA Replication (what is made, location, enzymes, semi-conservative, direction)

A
  • DNA–>DNA
  • Location: nucleus
  • Semi-conservative: one old strand, one new strand
  • Bidirectional
  • Enzymes involved:
    • Helicase: unwind double helix
    • DNA Polymerase: add nucleotides to each unwound string of DNA
      • can only add in 5’ –> 3’ direction
39
Q

Protein Synthesis

A

Central dogma of molecular biology

DNA —> mRNA —> protein

40
Q

DNA —> mRNA

A

transcription

41
Q

mRNA —> protein

A

translation

42
Q

Transcription (what is made, location, enzymes)

A
  • DNA–> mRNA
  • Location: nucelus
  • Enzymes involved:
    • RNA polymerase: unwinds DNA, makes a complimentary RNA strand to DNA
43
Q

Genetic Code (codes for, how many codons, start/stop codons)

A
  • mRNA language are codons (groups of 3 nucleotides)
  • each codes for:
    • amino acid (sense)
    • stop-signal (non-sense)
  • 64 possible codons, but only 20 amino acids
    • Degeneracy: multiple codes for one amino acid
  • Start codon: AUG (methionine)
  • Stop codons: UAG, UAA, UGA
44
Q

Translation (what is made, location, organelle involved)

A
  • mRNA –> protein
  • Location: cytoplasm
  • organelle involved: ribosome
45
Q

Translation Process

A
  1. mRNA becomes associated with ribosome
  2. start codon is exposed, and tRNA with complimentary anticodon binds
    - tRNA have a specific anticodon and are attached to a specific aa
  3. next codon of mRNA is exposed and tRNA binds
  4. peptide bond forms between aa
  5. ribosome moves along mRNA to expose another codon
  6. process repeats until stop codon

Physiology Exam #1 (5 decks)

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