Exam 1 (Objectives) Flashcards

1
Q

diameter of a prokaryotic cell

A

1-10microm

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2
Q

diameter of a eukaryotic cell

A

5-100microm

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3
Q

diameter of a bacterial ribosome

A

20nanom

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4
Q

diameter of a eukaryotic ribosome

A

25-30 nanom

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5
Q

diameter of globular protein

A

3.6nanom

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6
Q

What are the three kingdoms?

A

Bacteria, Archaea, Eukarya

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7
Q

What are the • 4 main classes of biological compounds?

A

carbohydrates, lipids, proteins, and nucleotides

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8
Q

What are carbohydrates made of?

A

made up of monosaccharides

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9
Q

What are lipids made of?

A

made of long hydrocarbon chain

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10
Q

What are proteins made of?

A

made of amino acids, amino acids are made up of carboxyl group, amino group, C center, H, and R group

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11
Q

What are nucleic acids made of?

A

made up of nucleotides (Adenine, Thymine, Guanine, Cytosine and Uracil) which contains 5 carbon based sugar and 3 phosphate group

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12
Q

Geometric isomers

A

isomers that switch the placement of functional groups between the two carbons bonded by a double bond

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13
Q

Stereoisomers

A

mirror image of one another that cannot be placed on top of one another to give the same image

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14
Q

chiral centers

A

carbon atoms with four different substituents are asymmetric

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15
Q

photosynthesis

A

energy from sun used to drive electrons from H2O -> CO2 which forms glucose and releases oxygen

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16
Q

Relate water structure to the hydrophobic effect.

A

Nonpolar solutes interact poorly with water so water cages the solute. The positive/negative dipole side of the water molecule will cage around the nonpolar solute.

17
Q

solubility of amphipathic molecules

A

hydrophobic region will be caged by water molecules to have a stronger hydrophilic attack

18
Q

solubility of nonpolar molecules

A

poorly soluble because water is a strong polar molecule; no polar = cannot be torn apart

19
Q

solubility of ionic compounds

A

highly polar, highly soluble

20
Q

Explain why buffers work.

A

Buffers are able to resist pH change because their conjugate acid and conjugate base are both present in great enough amounts to neutralize other acids and bases

21
Q

physiological pH

A
  • pH of blood is maintained by CO2 and CO3-
  • Respiratory acidosis: kidneys increase retention of HCO3-
  • Metabolic acidosis: lungs blow off CO2
22
Q

examples of quaternary structure

A

hemoglobin, collagen

23
Q

Properties of Peptide Bonds

A

•Planar due to double bond character in the resonance
structure
•Dipole moment due to the electrophilic nature of the carbonyl carbon
•Trans configuration of R groups due to steric restrictions

24
Q

primary structure of protein

A

sequence of amino acids from amino terminal to carboxyl terminal

25
classifications of amino acids
nonpolar or aliphatic, aromatic, polar or uncharged, positively charged, negatively charged
26
Common secondary structures
α helix β sheet β turn
27
α Helix
Forms by hydrogen bonding between carbonyl oxygen and the n+4 amino hydrogen
28
β Sheets
Consist of Adjacent Strands of Polypeptide; Stabilized through hydrogen binding between adjacent strands
29
Tertiary Structure
Form by self-assembly of secondary structures
30
Quaternary Structure
Structure of a protein that is composed of two or more polypeptide chains
31
enzymes
They participate in reactions without being consumed. They are not needed for the reaction to occur, but they help make the reaction go faster, hence they are biological catalysts.
32
specificity of enzymes
each enzyme can only catalyze a single reaction (or a group of reactions); this is caused by the specific reaction between enzymes and the substrate
33
simple enzymes
composed wholly of protein
34
complex enzymes
composed of protein and a cofactor; the complete enzyme is called a holoenzyme
35
Name the six enzyme classes
1. Oxidoreductase 2. Transferases 3. Hydrolases 4. Lyases 5. Isomerase 6. Ligase
36
interactions that hold protein together
covalent bonds, vander waals, hydrophobic, electrostatic, and hydrogen
37
allostery
the change in binding site conformations after a single ligand binds to an allosteric site on the protein