Lecture 2 Biomolecules and protein synthesis Flashcards

(31 cards)

1
Q

Chemical Bonds

A

Types:

  1. Ionic Bond
  2. Covalent Bong
  3. Hydrogen Bond
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2
Q

Ionic Bond

A

-Electron is transferred from one element to another

Electronegativity:one stong one weak- between two ions with Opposite charges
Ex.NacL

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3
Q

Covalent Bong

A

-Electrons are shared
-Electronegativity:Relativley Equal
1.Non-polar:Equal sharing
Ex.cH4
2.Polar:Unequalsharing
Ex.H2O

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4
Q

Hydrogen

A

-Opposite partial charges on adjacent molecules>Attraction

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5
Q

Biomolecules

A
  • Molecules synthesized by cells
  • Contain C-C covalent Bonds
  • Often make ring or chain structures
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6
Q

How do make Biomolecules

A

Dehydration synthesis

-Forming covalent Bond with Removal of water.

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7
Q

How do we Break Biomolecules

A

Hydrolysis

-Breaking covalent bond by adding water

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8
Q

Types of Biomolecules

A
  1. Carbohydrates
  2. lipids
  3. protiens
  4. Nucleic acids
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9
Q

Carbohydrates

A

Contain: C,H and Oxygen
C+H20
properties polar>Hydrophilic

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10
Q

Simple Sugar

A
Function: Fast Energy
1.Monosaccaride;one sugar
Ex.Glucose,Fructose
2.Disaccharides;2 sugars
Ex.Sucrose,lactose
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11
Q

Complex Carbohydrates

A
Function:-Energy storage
-structural Support
-component of cell membranes
Types:
polysaccharide: chain of sugars
Ex.Starch,glycogen,cellulose,chitin
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12
Q

Lipids

A

contain:C, H,and oxygen
properties:
-Non-polar > hydrophobic:Does not dissolve in water

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13
Q

Types of Lipids

A
  1. Triglycerides
  2. phospholipids
  3. Eicosanoids
  4. steroids
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14
Q

Tryglicerides

A
Structural:
1.glycerol
2.3 fatty acid chains
Function:
-Energy storage
-insulation
-protection
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15
Q

Types of triglycerides

A
-Saturated:
no double bond
tightly packed
solid at root temp
-Unsaturated
contain double bond
loosely packed
liquid at noon tem
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16
Q

phospholipids

A
Structure:
-glycerol
-phosphate group (polar)
-Fatty acid tails(non-polar)
Function:
-membrane structure
17
Q

eicosanoids

A
Structure:
-ring structure 
-Fatty Acids
function:cellular communication
Ex.prostaglandin(pain)
18
Q

Sterols

A
structure:
-4 carbon rings with side chain
-all derived form cholesterol
Function;
membrane fluidity
cellular communication
others
Ex.cholesterol,testosterone,Vitamine D
19
Q

Protients

A
contain:C,H,O,N
Structure:chain of amino acids(polypeptide)
Function:
-structuralSupport
-Enzymatic Activity
-Chemical messengers
-Receptors
20
Q

Amino Acids

A

Structure:

  • central(C) carbon
  • amino group:NH2
  • Carboxyl group:COOH
  • R Group:Determines amino acid
21
Q

Protein structure Levels

A
Primary;sequence of aa (peptide bond)
secondary:structural motifs(h-bond)
1 alpha Helix:spirals
2.Beta pleated sheet:pleats
3.tertiary:large scale motifs formed
by interactions between R group
4.quaternary:-bonding with multiple peptide chin
22
Q

Nucleic Acids

A
contain C,H,O,N,P
properties:polar>hydrophilic
Structure;chain of nucleotides
Function:
1.store Genetic Info(DNA)
2.DNA expression(RNA)
23
Q

nucleotide

A

1.Phosphate group
2.Sugar
3.Nitrogenous base
-adenine, guanine, cytosine,thymine(DNA) or Uracil(RNA)
complementary base pairing:A-T(DNA)or A-U(RNA)

24
Q

DNA

A
  • Double stranded helix
  • sugar:deoxyribose
  • Thymine binds to adenine
25
RNA
- Single Stranded - sugar :ribose - Uracil bind to adenine
26
3 types of RNA
1. mRNA:messenger RNA,nucleus > Ribosome 2. tRNA:tranport RNA, important in protein synthesis 3. rRNA:ribosomal RNA, part of the Ribosome
27
DNA Replication
Location:nucleus -semi conservative:one old strand one new strand -Bidirectional Enzymes involved Helicase:unwnd double helix DNA polymerase:add nucleotides to ech unwind string to DNA can only add in 5 to 3 Direction
28
protein Synthesis
-central dogma of molecular biology DNA to mRNA to Protein Transcription. Translaton
29
Transcription
DNA to m RNA location:Nucleus Enzymes involved -RNA polymerase;Unwinds DNA,makes a complimentary RNA strand to DNA
30
Translation
mRNA to Protein location: cytoplasm - organels involved ;Ribosomes(ribosomal RNA)
31
process of translation
1. mRNA becomes associated with a ribosome 2. Start Codon is exposed, and tRNA with complimentary anticodon-tRNA have a specific anticodon, and are attached binds to an amino acid 3. Next codon of mRNA exposed and tRNA binds 4. peptide bond forms between 2 amino acids 5. Ribosomes move along mRNA to expose another codon 6. process repeats until stop codon