Lecture 2.5 For 2.5 Quiz Flashcards

1
Q

Saturated Fats

A
  • Solid at room temp
  • Even number of Carbon’s and single covalent bonds
  • Butter on Table
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2
Q

Unsaturated fats

A
  • Better for you
  • Olive Oil
  • </= 1 double covalent bonds
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3
Q

Phospholipids

A
  • Similar to triglycerides
  • 1 fatty acid replaced by molecule with P and N
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4
Q

What is meant by Polarity?

A
  • Hydrophilic: Polar (think Polar bears)
  • Hydrophobic: NonPolar
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5
Q

What does amphipathic mean in reference to the phoso. bilayer

A
  • Phobic and Philic side
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6
Q

Steroids

A

(Cholesterol–>bile salts, estrogen, progesterone, testosterone)

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7
Q

Carboxylic Acid Group

A

COOH

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8
Q

Amino Group

A

NH2

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9
Q

ID Protein by…

A

Central Caron atom, amino acids, amino group, carboxylic group, and side chains

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10
Q

mRNA

A
  • Messenger RNA
  • Contains genetic information copied from a portion of DNA
  • Carries genetic information from gene our of nucleus into the cytoplasm (then turns into protein)
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11
Q

tRNA

A
  • Transfer RNA
  • Transports amino acids to the riosomes during PS
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12
Q

rRNA

A
  • Ribosomal RNA
    -Does NOT contain genetic information
  • Structural component of ribosomes
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13
Q

RNAi

A
  • RNA interference
  • at molecular level–>gene control, turn off gene (inhibits gene exression)
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14
Q

Peptide Bond

A
  • Bond between amino acids
  • di, tri, poly, etc.
  • 50-3K AA’s (proteins)
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15
Q

1° Structure

A
  • Determined by a sequence of AA’s with peptide bonds
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16
Q

2° Structure

A
  • Folds/twists/bends in polypeptide bonds caused by hydrogen bonds (helices/pleats)
  • H helps the twists, no kinks yet
17
Q

3° Structure

A

-Folds of the helices/pleats, SOme AA’s (polar) remain unfolded(philic) others fold inwards (Phobic)

18
Q

Domain Shape

A

100-200 AA’s of protein: changes in 1°/2°–> changes protein function

19
Q

4° Structure

A

> /= 2 proteins associate for function: spatial relationship between individual subunits exist

20
Q

Enzymes are…

A
  • Protein catalysit that speeds up chem reactions by lowering activation energy: not changing enzyme permanently
21
Q

Lock and Key Model

A
  • Reactants (key) and to active site (lock) on enzyme
22
Q

Induced Fit Model

A
  • Enzyme changes shape to fit reactants etter
  • Doesn’t have to be perfect fit
  • Some render enzyme useless (temp., physical shape, pH)
23
Q

Lipase

A

Breakdown of lipids

24
Q

Protease

A

Breakdown of proteins

25
Q

DNA

A
  • Deoxyribose
  • A,T,G,C
  • Antiparallel
26
Q

RNA

A
  • Ribose
  • 1 more oxygen than deoxyribose
  • A,U,G,C
27
Q

Purines

A
  • Adenine (2 circles)
  • Guanine (2 circles)
28
Q

Pyrimidines

A
  • Thymine (1 circle)
  • Uracil
  • Cytosine (1 circle)
29
Q

Nucleotides

A
  • Sugars, nitrogenous bases, phosphate backbone
  • Monomer of Nucleic Acids
30
Q

Protein Synthesis

A
  • 2 steps
  • 1st Transcription
  • 2nd Translation
  • Always in the Nucleus
    -CDB is PS
  • DNA–>(Transc)(mRNA)–>(transl)(protein)
31
Q

Central Dogma of Biology

A
  • Involved in gene expression like PS
  • DNA indirectly dictates protein function–>import cellular function
  • When genes become active–> an enzyme makes a temp. RNA copy of the information (Think CD/DVD)
32
Q

DNA Rep.
Transcription
Translation

A
  • Nucleus
  • Nucleus
  • Cytoplasm
33
Q

ATP is..

A
  • Important energy molecule
  • Adenine and Ribose make up ATP
  • A, Ribose, 3 phosphate groups
34
Q

When bonds break between 2nd and 3rd p group on ATP creates…

A

Energy