AP Biology Ch 3

Helpfulness: 0
Set Details Share
created 8 years ago by chemistry_goo
291 views
Grade levels:
6th grade, 7th grade, 8th grade, 9th grade, 10th grade, 11th grade, 12th grade, College: First year, College: Second year, College: Third year, College: Fourth year
show moreless
Page to share:
Embed this setcancel
COPY
code changes based on your size selection
Size:
X
Show:
1

DNA

The fundamental hereditary material of all living organisms.

2

RNA

An often single-stranded nucleic acid whose nucleotides use ribose rather than deoxyribose and in which the base uracil replaces thymine found in DNA. Serves as genome from some viruses.

3

Nucleotide

The basic chemical unit in nucleic acids, consisting of a pentose sugar, a phosphate group, and a nitrogen-containing base.

4

Base

The purine or pyrimidine that is attached to each sugar in the sugar-phosphate backbone.

5

Pyrimidine

One of the 2 types of nitrogenous bases in nucleic acids. Each of the pyrimidines- cytosine, thymine, and uracil- pairs with a specific purine.

6

Purine

One of the 2 types of nitrogenous bases in nucleic acids. Each of the purines- adenine and guanine- pairs with a specific pyrimidine.

7

Deoxyribose

A 5-carbon sugar found in nucleotides and DNA.

8

Ribose

A 5-carbon sugar in nucleotides and RNA.

9

Phosphodiester linkage

The connection in a nucleic acid strand, formed by linking 2 nucleotides.

10

Adenine (A)

A nitrogen-containing base found in nucleic acids, ATP, NAD, and other compounds; bonds with Thymine; purine.

11

Cytosine (C)

A nitrogen-containing base found in DNA and RNA; pairs with Guanine; pyrimidine.

12

Guanine (G)

A nitrogen-containing base found in DNA, RNA, and GTP; pairs with Cytosine; purine.

13

Thymine (T)

Nitrogen-containing base found in DNA; pairs with Adenine; pyrimidine.

14

Uracil (U)

A pyrimidine base found in nucleotides of RNA.

15

Complementary base pairing

The AT (or AU), TA (or UA), CG, and GC pairing of bases in double-stranded DNA, in transcription, and between tRNA and mRNA.

16

Genome

The complete DNA sequence for a particular organism or individual.

17

Gene

A unit of heredity. Used here as the genetic function which carries the information for a polypeptide or RNA.

18

Enzymes

Catalytic proteins that speed up biochemical reactions.

19

Defensive proteins

Recognize and respond to substances or particles that invade the organism from the environment (antibodies).

20

Hormonal and regulatory proteins

Control physiological processes; insulin.

21

Receptor proteins

Receive and respond to molecular signals from inside and outside the organism.

22

Storage proteins

Store chemical building blocks- amino acids- for later use.

23

Structural proteins

Provide physical stability and movement; collagen.

24

Transport proteins

Carry substances within the organism; hemoglobin.

25

Genetic regulatory proteins

Regulate when, how, and to what extent a gene is expressed.

26

Amino acid

An organic compound containing both NH2 and COOH groups. Proteins are polymers or amino acids.

27

R group

The distinguishing group of atoms of a particular amino acid; also known as a side chain.

28

Disulfide bridge

The covalent bond between two sulfur atoms (-S-S-) linking 2 molecules or remote parts of the same molecule.

29

Peptide linkage

The bond between amino acids in a protein; formed between a carboxyl group and amino group (-CO-NH-) with the loss of water molecules.

30

Primary structure

The specific sequence of amino acids in a protein.

31

Secondary structure

Of a protein, localized regularities of structure, such as the alpha helix and beta pleated sheet.

32

Alpha helix

A prevalent type of secondary protein structure; a right-handed spiral.

33

Beta pleated sheet

A type of protein secondary structure; results from hydrogen bonding between polypeptide regions running antiparallel to each other.

34

Tertiary structure

The relative locations in 3D space of all the atoms in the molecule. The overall shape of a protein.

35

Denaturation

Loss of activity of an enzyme or nucleic acid molecule as a result of structural changes induced by heat or other means.

36

Quaternary structure

The specific 3-dimensional arrangement of protein subunits.

37

Catalyst

A chemical substance that accelerates a reaction without itself being consumed in the overall course of the reaction. Catalysts lower the activation energy of a reaction. Enzymes are biological catalysts.

38

Transition state

In an enzyme-catalyzed reaction, the reactive condition of the substrate after there has been sufficient input of energy (activation energy) to initiate the reaction.

39

Activation energy

The energy barrier that blocks the tendency for a chemical reaction to occur.

40

Substrate

The molecule or molecules on which an enzyme exerts catalytic action.

41

Active site

The region on the surface of an enzyme or ribozyme where the substrate binds, and where catalysis occurs.

42

Enzyme-substrate complex (ES)

An intermediate in an enzyme-catalyzed reaction; consists of the enzyme bound to its substrate(s).

43

Cofactors

Inorganic ions such as copper, zinc, and iron that bind to certain enzymes.

44

Coenzyme

A carbon-containing molecule that is required for the action or one or more enzymes. It is usually relatively small compared with the enzyme to which it temporarily binds, and it adds or removes chemical groups from the substrate.

45

Prosthetic groups

Distinctive, non-amino acid atoms or molecular groupings that are permanently bound to their enzymes.

46

Saturated

The enzyme is working at its maximum rate.

47

Competitive inhibitor

A nonsubstrate that binds to the active site of an enzyme and thereby inhibits binding of its substrate.

48

Noncompetitive inhibitor

A nonsubstrate that inhibits the activity of an enzyme by binding to a site other than its active site.

49

Allosteric regulation

Regulation of the activity of a protein (usually an enzyme) by the binding of an effector molecule to a site other than the active site.

50

Feedback inhibition

A mechanism for regulating a metabolic pathway in which the end product of the pathway can bind to and inhibit the enzyme that catalyzes the first committed step in the pathway. Also called end-product inhibition.

51

Isozymes

A group of enzymes that catalyze the same reaction but have different chemical compositions and physical properties.