bio unit 1 Flashcards

(37 cards)

1
Q

macromolecules

A

large amount of molecules

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2
Q

polymers

A

chain of molecules not limited in length, a bunch of monomers

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3
Q

dehydration synthesis

A

monomer bonds to monomer with a covalent bond, H + OH removed from the monomers, so water is a byproduct, result is a polymer

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4
Q

hydrolysis

A

polymers broken down into monomers, covalent bonds broken, water is hydrolyzed, H + OH subcomponents are added back to either monomer, reverse of dehydration synthesis

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5
Q

organic molecules

A

nucleic acids, proteins, carbohydrates, lipids

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6
Q

carbs

A

C,H,O

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7
Q

function of carbohydrates

A

energy storage, structure of the cell, cellular communication

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8
Q

structure of carbs

A

3+ carbons, 2+ oxygens, multiple hydrogens

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9
Q

monosaccharide

A

monomer of carbs, contain C,H,O in a 1:2:1 ratio

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10
Q

polysaccharide

A

polymer of carbs, long chains of monosaccharides

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11
Q

glucose chains examples

A

glycogen, starch, cellulose

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12
Q

structure and function of starch

A

stores energy, digested v. easily, can dissolve

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13
Q

structure and function of cellulose

A

makes cell walls, not easily digested, cannot dissolve

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14
Q

why are starch and cellulose so different if their components are so similar?

A

in starch every glucose is oriented in the same direction, in cellulose every other glucose is flipped upside down in 180*

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15
Q

proteins

A

C,H,O,N,(S)

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16
Q

monomer of proteins

17
Q

polymer of proteins

A

amino acid chains, polypeptides, proteins

18
Q

structure of amino acid

A

amino group, R group, carboxyl group, connected via peptide bond

19
Q

peptide bond

A

forms between C of carboxyl group of 1 amino acid, and the N of the amino group of another amino acid

20
Q

4 levels of protein structure

A
  1. Primary Structure
  2. Secondary Structure
  3. Tertiary Structure
  4. Quaternary Structure
21
Q

Primary Structure

A

specific sequence of amino acids (w/ peptide bonds)

22
Q

Secondary Structure

A

based on backbone interactions that will create helices or pleat shapes due to hydrogen bonds

23
Q

tertiary structure

A

r group interactions, influence overall structure + shape of the protein

24
Q

disulfide bonds

A

form between the 2 amino acids w/ sulfur, this is the strongest r group interaction

25
r-group characteristics
significant if protein mutations occur, if the properties change then so does the shape of the protein, if the shape changes then the function does too
26
quaternary structure
protein complexes form when 2 or more polypeptides work together
27
Nucleic Acids
C,H,O,N,P
28
monomer of nucleic acids
nucleotide
29
structure of nucleotide
pentose sugar, phosphate group, nitrogenous base
30
purine
nitrogenous base with 2 rings ex. adenine and guanine
31
pyrimidines
nitrogenous base with 1 ring ex. cytosine, thymine, uracil
32
ATP
adenosine triphosphate, a nucleotide of a nucleic acid, a monomer but does not bond with other ATPs to make a polymer
33
function of ATP
energy currency, holds onto energy for a little while and then spends it
34
structure of ATP
ribose sugar, nitrogenous base (always Adenine), 3 phosphate groups
35
polymers of nucleic acid
DNA + RNA
36
structure of DNA + RNA
double/ single helix
37
function of DNA + RNA
to store information, stored as a specific sequence of nitrogenous bases