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Science > Unti 2: The Big Four > Flashcards

Unti 2: The Big Four Flashcards

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0
Q

Inorganic molecules

A

Def.- substances that do not contain carbon
+ exceptions (CO, CO2, CO2-)
3

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1
Q

Organic molecules

A 
Def.- any molecule that contains carbon 
Exceptions- CO (carbon monoxide)
CO2 (carbon dioxide)
CO2- ( carbonate)
     3
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2
Q

Polymers

A

Smaller organic molecules join into long chains

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3
Q

Monomers

A

Individual unit that builds up polymers

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4
Q

Macromolecules

A

Very large molecules

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5
Q

Dehydration synthesis

A

A reaction that removes molecules of water to form polymers and monomers

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6
Q

Hydrolysis

A

The reaction that adds water to polymers to separate them to their individual monomers

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7
Q

The big four

A
  • macromolecules of life
  • lipids(fats)
  • carbohydrates
  • proteins
  • nucleic acids(DNA and RNA)
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8
Q

Carbonhydrates

A

Def.- molecules that form from atoms in 1C:2H:1O ratio

-monomers= monosaccharide(simple sugars)

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9
Q

Monosaccharides

A
  • usually sweet, white powdery substances(fructose, glucose) that form rings of carbon atoms
  • function= serve as a direct, quick source of energy for living organisms during cellular respiration, and building blocks of polymers
  • glucose
  • fructose
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10
Q

Disaccharide

A
  • two monosaccharide molecules combine by dehydration synthesis to form disaccharides z
  • important sources of energy when broken down into the body
  • lactose(found in milk sugar)
  • maltose(in grains)
  • sucrose( table sugar)
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11
Q

Polysaccharides

A

Def.- many(tens to hundreds) units of monosaccharides combine by dehydration synthesis

  • separate into monosaccharides by hydrolysis
  • starch= many glucose units, storage of energy polysaccharide in plants
  • glycogen= important storage polysaccharide in animals
  • cellulose= many glucose units, ridged structure in plant cell walls
  • chitin= some nitrogen containing monosaccharides, solid structure of arthopods and fungi
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12
Q

Indicators of carbonhydrates

A
  • Lugol’s solution—> originally brown—> in starch turn black/blue
  • Benedict solution—> originally blue—> monosaccharides turn it yellow/orange
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13
Q

Lipids

A

Def.- diverse group of molecules that are no polar and generally do not dissolve in water

  • they mostly contain carbon, hydrogen, very few molecules of oxygen atoms, but some also have phosphorous
  • simple lipids
  • phospholipids
  • sterols
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14
Q

Simple lipids

A

Def.- very large molecule that form 2 different kinds of monomers by dehydration synthesis

  • 3 fatty acids(long chains of carbon with oxygen at the end*saturated or unsaturated) and 1 glycerol(smaller 3-carbon compound)
  • storage materials
  • mechanical protection
  • insulation
  • dissolve vitamins A,D,E,K
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15
Q

Phospholipids

A

Def.- a lipid that contains phosphate

  • their monomers= 1 glycerol, 2 fatty acids(saturated or unsaturated), phosphate<— dehydration synthesis
  • form borders of all cell membranes
  • participate in forming many cell organelles
  • partially polar, partially nonpolar*
16
Q

Sterols

A

Def.- highly nonpolar(hydrophobic) group of molecules. Formed from 4 rings of carbon atoms. One ring is made up of five carbons,cthe other three rings are made up of six carbons

  • cholesterol= important component of cell membrane
  • sex hormones= normal development of sexual functions, muscle and body hair formation
  • vitamin D= normal bone formation, immune functions
  • digest fats
17
Q

Indicators of lipids

A
  • Sudan III indicator—> dark red/brown—> in lipids turns bright red
  • brown bag test–> if lipids are dropped on a brown paper bag they stain the bag
  • emulsion–> lipids+alcohol shaken together and mixed with water, thy form a white emulsion
18
Q

Proteins

A
  • monomers= amino acids

- made of three groups Carboxyl functional group, amino acid functional group, R group

19
Q

R group

A
  • the R group can be 20 different kinds of side chains, so we have 20 different types of amici acids in our body
  • the R group determines the characteristics of the amino acid
20
Q

Amino acids

A
  • some are essential( our body cannot make them so we need to take them in with food) while other are nonessential(we can make these)
  • two amino acids can combine at their amino and Carboxyl ends by dehydration synthesis. They form a peptide bond together
  • the product of this reaction is a dipeptide(2 amino acids), polypeptide(many amino acids)
21
Q

Primary structure of a protein

A

Once the proper number of amino acids combine by peptide bond, we get a polypeptide chain( the number and types of amino acids combined to form a polypeptide that eventually folds into a protein)

22
Q

Secondary structure of a protein

A
  • alpha helix= if the H-bonds form within the polypeptide chain, a spiral staircase shape is formed
  • beta pleaded sheet= if the H-bonds form between longer stretches of polypeptide chains a long fan shape is formed
23
Q

Tertiary structure

A

All kinds of chemical bonds(covalent, ionic, disulfide bridge, H-bond, van der waals attraction, dipole-dipole interactions) are used to from the 3 dimensional structure of the polypeptide chain. If the protein is made up of only one polypeptide chain than this is the final structure of the protein.

24
Q

Quaternary structure

A

If a protein is made up of more than one polypeptide chain, they are connected by various bonds during the quaternary structure of the protein

25
Q

Enzymes

A

Function of protein

- catalyze reactions in the body (speed up digestion of fats)

26
Q

Structural proteins

A

Function of proteins

- support various structures(cocoon, hair, horns, feathers, spider silk)

27
Q

Storage proteins

A

Function of proteins

- proteins in milk, eggs, seeds

28
Q

Transport proteins

A

Function of proteins

- like hemoglobin, carry molecules

29
Q

Hormones

A

Function of proteins

- regulate growth, development, metabolism

30
Q

Receptors

A

Function of proteins

- detect signals from the enviroment

31
Q

Motor proteins

A

Function of proteins

- like muscle, move organism or substances inside

32
Q

Defensive proteins

A

Function of protein

- antibodies that fight against bacteria and viruses

33
Q

Denaturation of proteins

A
  • proteins are very sensitive to a wide range of environmental factors
  • denaturation= when the protein structure is destroyed opbecuas elf an environmental factor
  • proteins are denatured:
  • pH = too high or too low pH
  • temperature= too high
  • concentration of certain salts is too high
34
Q

Indicators of proteins

A
  • biuret reagent—> originally blue—> proteins tun it purple/lavender
35
Q

Nucleic acids

A

Def.- macromolecules with complex monomers called nucleotides

36
Q

Nucleotides

A
  • formed from three smaller components
  • monosaccharides with five carbon atom- ribose of deoxyribose
  • phosphate ion= PO3-/4
  • nitrogen containing bases( adenine=A, guanine=G, cytosine=C, and thymine=T or uracil=U)
  • function—> to build up nucleic acids, but they also participate in the processes of cellular respiration and photosynthesis
37
Q

DNA

A
  • one polymer of nucleotides is DNA
  • DNA has two polynucleotide chains combined with H-bonds at the base section of the nucleotide.
    A—>T
    G—>C
  • sugar is always deoxyribose in DNA
  • function= storage molecule for genetic information. DNA is able to copy itself and pass on the genetic material when a cell reproduces
38
Q

RNA

A
  • A, C, G, U
  • sugar is ribose
  • function= carry small segments of genetic info in the cell

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