Test 1

Question 1

4 raw materials needed for life

Answer 1

hydrogen, oxygen, nitrogen, and carbon

Question 2

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

Answer 2

molecular biology

Question 3

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

Answer 3

catalysis

Question 4

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

Answer 4

law of segregation

Question 5

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)

Answer 5

higher

Question 6

cell cycle composed of G1, S, and G2

Answer 6

Interphase

Question 7

chromosomes are decondensed and not visible

Answer 7

interphase

Question 8

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

Answer 8

S phase

Question 9

pairs of identical
chromosomes linked by a structure called
centromere.

Answer 9

sister chromatids

Question 10

Formation of the centrosome, the
nucleus disappears (mitosis)

Answer 10

prophase

Question 11

Alignment of chromosomes (mitosis)

Answer 11

Metaphase

Question 12

Separation of chromosomes at the
centromere (mitosis)

Answer 12

anaphase

Question 13

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

Answer 13

telophase

Question 14

abnormal
segregation of
chromosomes

Answer 14

nondisjunction

Question 15

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

Answer 15

one gene, one enzyme

Question 16

Nucleic acids are

Answer 16

polymers

Question 17

For ribonucleic acid and deoxyribonucleic acid, monomers are

Answer 17

nucleotides

Question 18

backbone of the molecule is provided by the

Answer 18

phosphate groups and sugars

Question 19

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.

Answer 19

methylation (adding ch3)

Question 20

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

Answer 20

RNA modifications

Question 21

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

Answer 21

protein modifications

Question 22

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

Answer 22

ionic bonds

Question 23

The formation of a chemical bond is an blank process

Answer 23

exothermic

Question 24

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

Answer 24

pi stacking

Question 25

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

Answer 25

configuration

Question 25

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

Answer 25

conformation

Question 26

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

Answer 26

stereoisomers

Question 27

stereoisomers that are one the mirror image of the other.

Answer 27

enantiomers

Question 28

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.

Answer 28

buffer solution

Question 29

Two major properties of buffer solutions

Answer 29

1. its ph 2. buffer capacity

Question 30

the sequence of amino acid residues in a polypeptide

Answer 30

primary strucuture

Question 31

the organized elements that favor folding

Answer 31

secondary strucuture

Question 32

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

Answer 32

tertiary structure

Question 33

the formation of multi-protein complexes

Answer 33

quaternary structure

Question 34

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

Answer 34

group 1- apolar proteins

Question 35

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

Answer 35

group 2- polar

Question 36

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

Answer 36

3rd group - negatively charged

Question 37

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

Answer 37

secondary structure

Question 38

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

Answer 38

structural motifs

Question 39

a whole, independent functional unit within a protein

Answer 39

domain

Question 40

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

Answer 40

protein folding

Question 41

The two major driving forces to achieve folding are

Answer 41

van der waal's interactions hydrophobic interactions

Question 42

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

Answer 42

protein disulfide isomerase

Question 43

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

Answer 43

ligand

Question 44

complementary to the ligand (physico-chemical properties!

Answer 44

a binding site

Question 45

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

Answer 45

conformational flexibility

Question 46

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!

Answer 46

induced fit

Question 47

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

Answer 47

cooperativity

Question 48

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

Answer 48

cofactor

Question 49

a coenzyme or inorganic cofactor covalently bound to an enzyme

Answer 49

prosthetic group

Question 50

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

Answer 50

holoenzyme

Question 51

the protein portion of an enzyme

Answer 51

apoenzyme

Question 52

the molecule that undergoes the enzyme-catalyzed reaction

Answer 52

substrate

Question 53

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

Answer 53

active site

Question 54

one enzyme usually catalyzes only one reaction

Answer 54

reaction specificity

Question 55

1/2 Vmax =

Answer 55

Km

Question 56

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

Answer 56

Michaelis-Menten equation

Question 57

Vmax =

Answer 57

Kcat [Et]

Question 58

Vo =

Answer 58

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

Question 59

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

Answer 59

allosteric proteins

Question 60

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

Answer 60

allosteric proteins

Question 61

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

Answer 61

Covalent modifications