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BIO 307 > Chapter 2 > Flashcards

Chapter 2 Flashcards

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Biology 101 flashcards
1
Q

Define atoms

A

Smallest unit of chemical elements

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2
Q

Covalent vs. Ionic bonds

A

Covalent bonds share valence electrons
Ionic bonds give away valence electrons (ion want it)

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3
Q

Non-polar Covalent Bonds

A

Electrons are shared equally

Lipid molecules have fatty acid tails
- not water soluble

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4
Q

Polar covalent bonds

A

Electrons are not shared equally; they have positive and negative ends
ex. Water

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5
Q

Cation + anions

A

In an ionic bond, one atom gives elections to another so that both have filled electrons

The electron donor is positively charged, now is called the cation

The electron receiver is positively charged, now is called the anion

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6
Q

Hydrophilic vs hydrophobic

A

Hydrophilic: molecules that can dissolve in water
Hydrophobic: molecule’s that repel water

Ionic bonds are much weaker than covalent, they easily dissociate when dissolved in H2O

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7
Q

pH

A

Water molecules break to form free hydrogen ions and hydroxide ions

(below 7 = acidic, above 7 = basic)

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8
Q

Buffers

A

Buffers stabilize H+ concentration in a solution.
In blood, 2 molecules stabilize pH:
1) bicarbonate (HCO3-) und carbonic acid (H2CO3)

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9
Q

Acidosis vs alkalosis

A
  • if blood falls below 7.35 pH, it is called acidosis
  • if blood rises above 7.45 pH, it is called alkalosis
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10
Q

Carbohydrates

A

Organic molecules containing carbon, hydrogen, and oxygen, ring shaped

CnH2nOn

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11
Q

Monosaccharide vs disaccharide vs polysaccharide

A

Monosaccharide: simple sugar, single ring
Disaccharide: 2 monosaccharides covalently bonded together
Polysaccharide: numerous monosaccharides
jointed together

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12
Q

Lipids

A

Consist of non-polar hydrocarbon chains and rings

Hydrophobic = lipophilic

Categories: Triglycerides, phospholipids, steroids

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13
Q

Triglycerides

A

Include fat and oil (diet), stored in adipose tissue

1 glycerol molecule joined with three fatty acids

Fatty acids: C and H chains

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14
Q

saturated vs unsaturated fats

A

saturated fats = single bond (solid at room temp)
unsaturated fats = double bond (liquid at room temp)

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15
Q

phospholipids

A

major component of cell membrane
polar head made up of phosphate
nonpolar tails made up of fatty acid

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16
Q

micelles

A

groups of phospholipids
(polar head faces water)

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17
Q

steroids

A

*only lipid with a ring structure
*cholesterol, sex etc.
*nonpolar and insoluble in water
*able to pass through cell membranes
*easy access to our DNA

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18
Q

anabolic steroids

A

*mimic testosterone
*increase protein synthesis and cellular tissue (muscle)
*increase cholesterol, blood pressure
*more blood flow to tissues, higher BP
*cancer too

19
Q

what determines the function of the protein

A

the structure determines the function of the protein

20
Q

how many different amino acids are there?

A

20 different amino acids

21
Q

what is the functional group of protein

A

*Amino Acid
*an amine group (carboxyl group and a functional group)

22
Q

what kind of bonds hold together the tertiary structure of a protein

A

weak bonds hold the tertiary structure together. It is easily denatured (unfolded) due to changes in pH or temperature

23
Q

What are amino acids linked with

A

Peptide bonds

24
Q

What is a glycoprotein composed of?

A

Protein + carbohydrate

25
Q

What is a lipoprotein composed of?

A

Protein + lipid

26
Q

What are the 3 macromolecules that make up the cell?

A

Lipids, Carbohydrates, and Proteins

27
Q

define enzymes

A

enzymes are biological catalysts:
1. increase rate of rxn
2. are not changed by the rxn (so it can be used again)
3. do not change the nature of the reaction (the rxn can ouccur without the enzyme, just slower rxn rate)

28
Q

activation energy

A

the energy required for the reactancts to engage in a reaction

29
Q

adding heat to a rxn

A

adding heat increases the likelihood of a rxn occuring = increases rxn rate

30
Q

catalysts

A

help the rxn occur at lower temperatures by lowering the required activation energy

31
Q

describe how enzymes work with conformation and active sites

A
  • each enzyme has a specifc conformation, with pockets that serve as active sites in the enzyme
  • the reactants are called substates, and they fit into the active site
32
Q

describe the 2 models of enzyme activity

A

lock and key model
Induced fit model: enzyme structural change (wraps around substrate)

33
Q

enzyme-substrate complex

A

temporary bonds form creating the enyzme-substrate complex

34
Q

enzyme activity

A

measured by the rate at which substrate is converted to product

35
Q

conditions that influence enzyme activity

A
  • temperature
  • pH
  • concentration of cofactors and coenzymes
  • concentration of enzyme and substrate
36
Q

effects of temperature on enzymes

A

an increase in temp will increase rate of rxn until the temp reaches above body temp. At this point the enzyme is denatured.

Sustained high fever = denatured proteins

37
Q

effects of pH on enzymes

A

enzymes exhibit peak activity within a narrow pH range = pH optimum
optimium pH reflects the pH of the fluid the enzyme is found in (stomach vs saliva)

38
Q

coenzymes

A
  • an additional small molecule to aid in the rxn
  • they transport hydrogen atoms and other small molecules between enzymes
39
Q

cofactors

A
  • metal ions (Ca2+, Mg2+, Mn2+, Zn2+)
  • help form the active site through a conformational change of enzyme or help in enzyme-substrate binding.
40
Q

substrate concentrations

A

as substrate concentration increases, rate of rxn increases until the enzymes become saturated.

41
Q

metabolic pathway

A
  • formed by many enzymes
  • most rxns are linked together in a chain or web
42
Q

allosteric inhibition

A
  • negative feedback
  • what is turned on must be turned off
  • main goal of allosteric inhibition: keep a specific final product from accumulating
43
Q

branch point

A
  • are often inhibited by a form of negative feedback in which one of the final products inhibits the branch point enzyme
  • a divergent pathway becomes favored (chocolate chip cookies to PB cookies)

BIO 307 (4 decks)

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