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DAT Bio Ch 1 Molecules and Fundamentals of Biology > Topic 1 Proteins > Flashcards

Topic 1 Proteins Flashcards

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1
Q
  • Contain carbon, hydrogen, oxygen, and nitrogen atoms (CHON)
  • Combine to form amino acids
  • Polymers of amino acids joined by peptide bonds
A

Protein

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2
Q
  • Link together to build polypeptides (or proteins)
  • The monomers of proteins and have the structure below:
  • There are 20 different amino acids, each with a different “R” group
A

Amino Acids

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3
Q
  • Refers to all the proteins expressed by one type of cell under one set of conditions
A

Proteome

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4
Q
  • Polymers of amino acids that are joined by peptide bonds through dehydration (condensation) reactions
  • Becomes an amino acid chain that contains two end terminals on opposite sides
A

Polypeptides

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5
Q
  • (amino terminus) the side that ends with the last amino acids amino group
A

N-terminus

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6
Q
  • (carboxyl terminus) the side that ends with the last amino acids carboxyl group
A

C-terminus

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7
Q
  • Sequence of amino acids
A

Primary Protein Structure

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8
Q
  • Intermolecular forces between the polypeptide backbone due to hydrogen bonding
  • Forms alpha helices and beta pleated sheets
A

Secondary Protein Structure

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9
Q
  • Tree-dimensional structure due to interactions between R-groups
  • Can create hydrophobic or hydrophilic spaces based on the R-groups
  • Disulfide bonds are created by covalent bonding between the R-groups of two cysteine amino acids
  • Non-covalent interactions: H-bonds, ionic bonds, hydrophobic effect, and Van Der Waals forces
A

Tertiary Protein Structure

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10
Q
  • Multiple polypeptide chains come together to form one protein
A

Quaternary Protein Structure

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11
Q
  • Not water soluble
  • Dominated by secondary structure
  • Made of long polymers
  • Maintain and add strength to cellular and matrix structures
A

Fibrous/Structural Quaternary Protein Structure

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12
Q
  • Water soluble
  • Dominated by tertiary structure
  • Enzymatic, hormonal, inter and intracellular storage, transport, osmotic regulation, immune response
A

Globular Quaternary Protein Structure

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13
Q
  • Proteins that function as membrane pumps, channels, or receptors
A

Intermediate Quaternary Protein Structure

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14
Q
  • Amino acids only
  • Albumins and Globulins
  • Scleroprotein
A

Simple Protein Composition

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15
Q
  • proteins that act as carriers or enzymes
A

Albumins and Globulins

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16
Q
  • fibrous proteins (I.e. collagen)
A

Scleroprotein

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17
Q
  • simple protein + non-protein
  • lipoprotein
  • mucoprotein
  • chromoprotein
  • metalloprotein
  • nucleoprotein
A

Conjugated Protein Structure

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18
Q
  • bound to lipid
A

Lipoprotein

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19
Q
  • bound to carbohydrate
A

Mucoprotein

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20
Q
  • bound to pigmented molecule
A

Chromoprotein

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21
Q
  • complexed around metal ion
A

Metalloprotein

22
Q
  • contains histone of protamine, bound to nucleic acid
A

Nucleoprotein

23
Q
  • Describes the loss of protein function and higher order structures
  • Reversed back to primary structure
  • Implies that all of the information needed is encoded in its primary structure
A

Protein Denaturation

24
Q
  1. High or low temperatures
  2. pH changes
  3. Solvent
A

Proteins denature due to

25
Q

Example: cooking eggs in high heat will disrupt the intermolecular forces in the egg’s proteins, causing it to coagulate

A

Protein Denaturation

26
Q
  • Eliminates whole protein structure including primary
A

Protein Digestion

27
Q
  1. storage
  2. hormones
  3. receptors
  4. motion
  5. structure
  6. immunity
  7. enzymes
A

Protein Functions

28
Q
  • Reserve of amino acids
A

Storage

29
Q
  • Signaling molecules that circulate through the body to regulate physiological process
A

Hormones

30
Q
  • Proteins in cell membranes, which bond to signal molecules to trigger changes inside cells
A

Receptors

31
Q
  • Movement generation for individual cells or entire organisms
A

Motion

32
Q
  • Provide strength and support to tissues
A

Structure

33
Q
  • Prevention and protection against foreign invaders
A

Immunity

34
Q
  • Act as biological catalysts by binding to substrates (reactants) and converting them into products
A

Enzyme

35
Q
  • Increase reaction rates by lowering the activation energy of a reaction
  • The transition state is the unstable conformation between the reactants and the products
  • Catalysts reduce the energy of the transition state
  • Do not shift a chemical reaction of affect spontaneity
A

Catalyst

36
Q
  • Act as catalysts by binding to substrates (reactants) and converting them into products
  • Bind to substrates at an active site, which is specific for the substrate that it acts upon
  • Most enzymes are proteins
  • Protein enzymes are susceptible to denaturation. They require optimal temperatures and pH for function
  • Catalyze reactions in forward and reverse directions
  • Do not change the spontaneity of a reaction
  • Almost always considered proteins, but RNA can act as an enzyme
A

Enzyme

37
Q
  • Measures how efficient and enzyme is at binding to the substrate and converting it to a product
A

Specificity Constant

38
Q
  • Describes how the active site molds itself and changes shape to fit the substrate when it binds
  • The “lock and key” model is an outdated theory of how substrates bind
A

Induced fit theory

39
Q
  • RMA molecule that can act as an enzyme (a non-protein enzyme)
A

Ribozyme

40
Q
  • Non-protein molecule that helps enzymes perform reactions by donating or accepting components
  • Organic cofactor (i.e. vitamins): coenzyme
  • Inorganic cofactors are usually metal ions
A

Cofactor

41
Q
  • Enzymes that are bound to their cofactors
A

Holoenzyme

42
Q
  • Enzymes that are not bound to their cofactors
A

Apoenzymes

43
Q
  • Cofactors that are tightly or covalently bonded to their enzymes
A

Prosthetic groups

44
Q
  • Occurs when a competitive inhibitor competes directly with the substrate for active site binding
  • The rate of enzyme action can be increased by adding more substrate
A

Competitive Inhibition

45
Q
  • Occurs when the noncompetitive inhibitor binds to an allosteric site that modifies the active site
  • In noncompetitive inhibition, the rate of enzyme action cannot be increased by adding more substrate
A

Noncompetitive inhibitor

46
Q
  • Location on an enzyme that is different from the active site
A

Allosteric site

47
Q
  • Can be used to visualize how inhibitors affect enzymes
A

Enzyme kinetics plot

48
Q

Terms used to describe the plot:

  • The x-axis represents substrate concentration [X]
  • The y-axis represents reaction rate or velocity (V)
  • Vmax is the maximum reaction velocity
  • Michaelis Constant (KM) is the substrate concentration [X] at which the velocity (V) is 50% of the maximum reaction velocity (Vmax)
  • Saturation occurs when all active sites are occupied, so the rate of reaction does not increase anymore despite increasing substrate concentration (causes graph plateaus)
  • Competitive inhibition: Km increases and Vmax stays the same
  • Noncompetitive inhibition: Km stays same while Vmax decreases
A

Enzyme kinetics plot

49
Q
  • Determined by substrate and enzyme concentration, temperature, pH, and presence/absence of inhibitors
A

Efficiency

50
Q
  • Catalyzes reactions that break the alpha-glycosidic bonds in starch
A

Amylase

DAT Bio Ch 1 Molecules and Fundamentals of Biology (34 decks)

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