bio unit 1 Flashcards

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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

A

amino acids

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
Q

r-group characteristics

A

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
Q

quaternary structure

A

protein complexes form when 2 or more polypeptides work together

27
Q

Nucleic Acids

A

C,H,O,N,P

28
Q

monomer of nucleic acids

A

nucleotide

29
Q

structure of nucleotide

A

pentose sugar, phosphate group, nitrogenous base

30
Q

purine

A

nitrogenous base with 2 rings ex. adenine and guanine

31
Q

pyrimidines

A

nitrogenous base with 1 ring ex. cytosine, thymine, uracil

32
Q

ATP

A

adenosine triphosphate, a nucleotide of a nucleic acid, a monomer but does not bond with other ATPs to make a polymer

33
Q

function of ATP

A

energy currency, holds onto energy for a little while and then spends it

34
Q

structure of ATP

A

ribose sugar, nitrogenous base (always Adenine), 3 phosphate groups

35
Q

polymers of nucleic acid

A

DNA + RNA

36
Q

structure of DNA + RNA

A

double/ single helix

37
Q

function of DNA + RNA

A

to store information, stored as a specific sequence of nitrogenous bases