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
Q

classifications of amino acids

A

nonpolar or aliphatic, aromatic, polar or uncharged, positively charged, negatively charged

26
Q

Common secondary structures

A

α helix
β sheet
β turn

27
Q

α Helix

A

Forms by hydrogen bonding between carbonyl oxygen and the n+4 amino hydrogen

28
Q

β Sheets

A

Consist of Adjacent Strands of Polypeptide; Stabilized through hydrogen
binding between adjacent strands

29
Q

Tertiary Structure

A

Form by self-assembly of secondary structures

30
Q

Quaternary Structure

A

Structure of a protein that is composed of two or more polypeptide chains

31
Q

enzymes

A

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
Q

specificity of enzymes

A

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
Q

simple enzymes

A

composed wholly of protein

34
Q

complex enzymes

A

composed of protein and a cofactor; the complete enzyme is called a holoenzyme

35
Q

Name the six enzyme classes

A
  1. Oxidoreductase
  2. Transferases
  3. Hydrolases
  4. Lyases
  5. Isomerase
  6. Ligase
36
Q

interactions that hold protein together

A

covalent bonds, vander waals, hydrophobic, electrostatic, and hydrogen

37
Q

allostery

A

the change in binding site conformations after a single ligand binds to an allosteric site on the protein