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Molecular Biology > Test 1 > Flashcards

Test 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

4 raw materials needed for life

A

hydrogen, oxygen, nitrogen, and carbon

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2
Q

can be defined as the study of essential macromolecules present in cells, including DNA,
RNA, and proteins, and the biological pathways between them

A

molecular biology

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3
Q

Chemical reactions are at the base of most of biological functions – they are based on energy
transfer

A

catalysis

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4
Q

When gametes are formed, there is an equal segregation of the alleles

A

law of segregation

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5
Q

for two genes located on the same chromosome, the further away they are, the (higher or lower) the chance they will not be linked during gametes formation (meiosis)

A

higher

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6
Q

cell cycle composed of G1, S, and G2

A

Interphase

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7
Q

chromosomes are decondensed and not visible

A

interphase

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8
Q

each chromosome is duplicated in this phase and the chromosome becomes a tetraploid

A

S phase

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9
Q

pairs of identical
chromosomes linked by a structure called
centromere.

A

sister chromatids

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10
Q

Formation of the centrosome, the
nucleus disappears (mitosis)

A

prophase

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11
Q

Alignment of chromosomes (mitosis)

A

Metaphase

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12
Q

Separation of chromosomes at the
centromere (mitosis)

A

anaphase

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13
Q

Division of the whole cell,
formation of new nuclei (mitosis)

A

telophase

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14
Q

abnormal
segregation of
chromosomes

A

nondisjunction

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15
Q

according to which each
gene codes for a specific polypeptide with
catalytic properties.

A

one gene, one enzyme

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16
Q

Nucleic acids are

A

polymers

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17
Q

For ribonucleic acid and deoxyribonucleic acid, monomers are

A

nucleotides

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18
Q

backbone of the molecule is provided by the

A

phosphate groups and sugars

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19
Q

a key modification in DNA. It occurs at the
nitrogenous bases and regulates DNA folding –
what is known as “chromatin state”. This has deep effects on gene expression.

A

methylation (adding ch3)

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20
Q

modifications vary more, and can affect also the sugars or include
substitutions of nitrogenous bases.

A

RNA modifications

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21
Q

modifications occur mostly at the R-group of selected amino acids.

A

protein modifications

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22
Q

can stabilize the three-dimensional structure of proteins and nucleic acids

A

ionic bonds

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23
Q

The formation of a chemical bond is an blank process

A

exothermic

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24
Q

he attractive, non-covalent interaction between the electrons of the pi orbitals of closely located molecules or functional
groups.

A

pi stacking

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25
Q

an arrangement of atoms which cannot be moved
without breaking and re-forming covalent bonds

A

configuration

25
Q

an arrangement that can change based on rotation
around an axis etc.

A

conformation

26
Q

two molecules sharing the same molecular formula but that cannot be superposed.

A

stereoisomers

27
Q

stereoisomers that are one the mirror image of the other.

A

enantiomers

28
Q

a system capable of resisting changes in pH, consisting of a conjugate acid-base pair in
which the ratio of proton acceptor to proton donor is near unity.

A

buffer solution

29
Q

Two major properties of buffer solutions

A
  1. its ph
  2. buffer capacity
30
Q

the sequence of amino
acid residues in a polypeptide

A

primary strucuture

31
Q

the organized
elements that favor folding

A

secondary strucuture

32
Q

the three-dimensional
organization of a protein, in domains and
motifs

A

tertiary structure

33
Q

the formation of
multi-protein complexes

A

quaternary structure

34
Q

group includes
amino acids with side
chains made of
hydrocarbon chains plus
methionine (which has a
thioether group)

A

group 1- apolar proteins

35
Q

Group of amino acids that can easily be involved in H-bonds/interact with water.

A

group 2- polar

36
Q

Aspartate and glutamate can be
involved also in salt bridges.
Amide group

A

3rd group - negatively charged

37
Q

Repeating structural elements with defined spatial properties,
held together by weak
interactions, particularly H-bonds

A

secondary structure

38
Q

specific arrangements
of secondary elements that can be found in
multiple proteins. They can represent a
whole domain or part of one.

A

structural motifs

39
Q

a whole, independent functional unit within a protein

A

domain

40
Q

The process through which a protein
reaches its native three-dimensional
conformation

A

protein folding

41
Q

The two major driving forces to achieve
folding are

A

van der waal’s interactions

hydrophobic interactions

42
Q

shuffles S-S bonds until the final conformation has been reached;

A

protein disulfide isomerase

43
Q

molecule bound to a protein (any kind of molecule, including another protein)

A

ligand

44
Q

complementary to the ligand (physico-chemical properties!

A

a binding site

45
Q

the “breathing” of a protein; small or large re-arrangements

A

conformational flexibility

46
Q

changes in the conformation of any macromolecule in response to ligand binding such that
the binding site of the macromolecule better conforms to the shape of the ligand – tighter binding!

A

induced fit

47
Q

in a protein complex, a change in the conformation of a protein subunit (like an enzyme)
in response to ligand (substrate) binding that renders that alters the binding affinity of the other subunits
to the ligand – e.g., increased affinity after the first ligand is bound to the first subunit

A

cooperativity

48
Q

can either be a metal ion or a coenzyme (metallo-organic molecule)

A

cofactor

49
Q

a coenzyme or inorganic cofactor covalently bound to an enzyme

A

prosthetic group

50
Q

an enzyme that includes all the molecules that make it active (cofactors etc)

A

holoenzyme

51
Q

the protein portion of an enzyme

A

apoenzyme

52
Q

the molecule that undergoes the enzyme-catalyzed reaction

A

substrate

53
Q

typically a pocket with a well-defined spatial orientation of chemical groups, amino
acids, or cofactors

A

active site

54
Q

one enzyme usually catalyzes only one reaction

A

reaction specificity

55
Q

1/2 Vmax =

A

Km

56
Q

V0 = (Vmax[S])/Km + [S]

A

Michaelis-Menten equation

57
Q

Vmax =

A

Kcat [Et]

58
Q

Vo =

A

(Kcat[Et][S])/Km + [S]

59
Q

undergo conformational changes as a consequence of the binding of a modulator (ligand)

A

allosteric proteins

60
Q

they have distinctive binding/kinetic properties
They show sigmoidal saturation curves

A

allosteric proteins

61
Q

occurring to the side chain (R group) of amino acid residues. Oftentimes these reactions directly involve ATP.

A

Covalent modifications

Molecular Biology (19 decks)

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