Unit I Flashcards

1
Q

adhesion

A

Attraction between unlike molecules

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2
Q

Cohesion

A

Attraction between like molecules

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3
Q

Specific heat

A

The amount of energy required to raise the temperature of one gram ph a substance by one degree Celcius

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4
Q

Heat of vaporization

A

The energy required to change one gram of water from a liquid to a gas

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5
Q

Functional groups

A

H, P, N, O, and S-containing groups commonly found in organic molecules

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6
Q

Amino functional groups

A

Attract hydrogen ions (protons) when in solutions. Function as bases. Link covalently with carboxyl groups to form amino acids.

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7
Q

Carboxyl functional groups

A

Release hydrogen ions (protons) when in solutions. Function as acids. Link covalently with amino groups to form amino acids.

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8
Q

Carbonyl functional groups

A

Site of reactions that link molecules (i.e. acetaldehyde, acetone) into larger, complex organic compounds.

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9
Q

Hydroxyl functional groups

A

Act as weak acids. Protons involved in acid-base reactions come from hydroxyl groups (on organic compounds). Hydroxyl groups are polar; organic compounds containing them will form hydrogen bonds and be soluble in water.

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10
Q

Phosphate functional groups

A

Carry negative charges on two oxygen atoms. When transferred from one organic to another, change in charge affects structure of recipient molecule. Phosphate groups bonded together store chemical energy.

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11
Q

Sulfhydryl functional groups

A

Can link to each other via disulfide (S-S) bonds.

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12
Q

Condensation/dehydration reactions

A

Polymerization of monomers. Results in the loss of water molecule.

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13
Q

Hydrolysis reactions

A

Breaks polymers apart by adding water molecule. More frequent than condensation/dehydration reactions.

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14
Q

Peptide bond

A

The bond that links amino acid together.

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15
Q

R-group

A

The “side chains” of amino acids that differentiates the 20 types of amino acid.

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16
Q

Oligopeptide

A

A polymer consisting of 50 or less linked amino acids.

17
Q

Polypeptide

A

A polymer consisting of 50 or more linked amino acids.

18
Q

Primary Structure

A

The unique sequence of amino acids making up a protein.

19
Q

Secondary Structure

A

Distinctively shaped sections of the linear sequence of a protein that are stabilized largely by hydrogen bonding that occurs between the oxygen on the carbonyl group of one amino acid residue and the hydrogen on the amino group of another.

20
Q

Tertiary Structure

A

Distinctive overall three-dimensional shape of a protein.

21
Q

Quaternary Structure

A

The combinations of polypeptides found in some proteins.

22
Q

Enthalpy

A

The total energy of a molecule, represented by H. Includes the potential energy in bonds and effect of molecule’s kinetic energy on pressure and volume.

23
Q

Entropy

A

The amount of disorder in a system, represented by S. Increases when products are less ordered than reactants.

24
Q

Chemical energy

A

A molecule’s potential to form stronger bonds; a type of potential energy.

25
Q

Gibbs free energy

A

The amount of energy in the reaction available to do work.

26
Q

Standard free-energy change equation

A

ΔG = ΔH – T ΔS

27
Q

Exergonic

A

When ΔG is less than 0; spontaneous.

28
Q

Endergonic

A

When ΔG is greater than zero; non-spontaneous.

29
Q

Transition state

A

The intermediate point between breaking old bonds and forming new ones.

30
Q

Substrates

A

Reactants which undergo a chemical reaction by binding to enzymes.

31
Q

Competitive inhibition

A

A regulatory molecule inhibits catalysts by competing with the substrate for access to enzyme’s active site.

32
Q

Allosteric

A

A regulatory molecule binds at a location other than the active site and changes the shape of the enzyme.

33
Q

Phosphodiester bond

A

The covalent bond formed between the phosphate group and 5-carbon sugars of DNA and RNA.

34
Q

Adenosine triphosphate (ATP)

A

The activated nucleotide used in construction of RNA.