Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Human Physiology + Cell and Molec Bio > Cell + Molec I > Flashcards

Cell + Molec I Flashcards

1
Q

Polar covalent bond

A

A covalent bond where one atom has the electron shared more often than the other, resulting in polarity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Hydrogen bond

A

the result of a polar covalent bond, hydrogen being attracted to a polar molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Hydrophobic or hydrophilic dissolves in water?

A

Hydrophilic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What two weak noncovalent bonds make up electrostatic attraction?

A

Hydrogen bonds and ionic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

4 types of weak noncovalent bonds

A

hydrogen bonding, ionic bonding, van der walls attractions (weak attractions b/w nonpolar moelcules), hydrophobic force: (nonpolar substances ushed together by water)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Hydronium vs hydroxyl

A

h3o+ and OH-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what are acids and bases

A

acids add Hydrogen ions to the water, bases accept

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what are fatty acids

A

hydrophobic lipids avec un hydrobcarbon tail and a carboxyl group (COO-)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

amino acid components

A

alpha carbon, amino group, carboxyl group, 1 of 20 residues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

nucleotid components

A

5-C ribose sugar, phosphate group, 1 of 4 nitrogenous bases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

how are polymers formed?

A

via condensation reactions of monomers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

how do you break apart polymers?

A

VIA hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

polysaccharide bonds

A

glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

single monomers of a polypeptide?

A

amino acids!

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

nucleic acid monomer

A

nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Metabolism

A

sum of all chemical reactions happening in a living system

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Catabolism

A

breakdown of molecules, releasing energy (cellular resp. is an example)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Anabolism

A

biosynthesis; assembles molecules using E (ex. photosynthesis)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

1st and second law of thermodynamics

A

E cant be made or destroyed, closed systems tend toward entropy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

-delta G and +delta G

A

favorable and unfavorable chemical reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Free energy vs Heat

A

useful and unuseful energy in a system

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

How does metabolism harvest energy?

A

metabolism: oxidizing organic molecules and building up large molecules through reduction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Oxidation vs reduction reactions

A

removal of electron, sometimes by adding oxygen, adding an electron, sometimes by removing oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Reduction oxidation reaction (redox reaction)

A

reducing something and oxidizing something else (oxidizing releases energy that then can be used for reduction)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What do enzymes lower?
activation energy
26
Catalyst
speed up chemical reactions without reacting or being used up
27
what do enzymes act upon
substrates
28
Equilibrium constant K
The ratio of reactant to product at equilibrium; higher means reaction is more favorable
29
what makes reactions go faster? (3)`
higher substrate to product concentration, higher temperature, more substrate concentration
30
Where does the enrgy to power unfavorable reactions come from
coupling favorable reactions with them
31
ATP name
Adenosine triphosphate
32
What is an activated carrier?
a small organic molecule that delivers energy for coupling; delivers one or more high energy bonds to a location
33
unfavorable: phosphorylation
Condensation of ADP to make phosphate bonds
34
Favorable: Hydrolysis of ADP
breaking bonds
35
What does Glutamine Synthase do?
Combine glutamic acid and ammonia to make glutamine; changes one aa to another (Uses STP to make glutamic acid into a higher energy state)
36
two examples of activated carriers
NADH and NADPH
37
what is NADPH used for?
light rxns in photosynthesis , Calvin cycle fixes CO2 to make sugar (Done by reducing NADP+ with hydrogen w 2 electrons)
38
what is NADH used for?
Catabolic rxns to synthesize ATP through cellular respiration
39
What BINDS to a protein?
A ligand
40
4 (1/2) levels of protein organization
aa sequence alpha helices and beta sheets helices sheets, loops and all (protein domains) interaction of multiple polypeptides
41
components of an amino acid
Central carbon, carboxyl group, aa side chain (residue), hydrogen, and amino group
42
what parts of an a.a. bind together in a condensation reaction
a carboxyl and amino group
43
Polypeptide backbone
repeating chain of N-C-C- that holds aas together
44
2 termini of an a.a. polypeptide
amino (N) terminus and a Carboxyl terminus (C)
45
What do chaperone proteins do?
speed up folding of proteins
46
what noncovalent interactions fold proteins?
electrostatic, Van der Waals, hydrophobic force,
47
What does secondary protein structure arise from?
the polypeptide backbone H-bonds
48
rigid structures of secondary organization
Alpha Helices; b/w C-O and N-H amino acids (1full turn is 3.6a.a.) Beta Sheets; backbone H-bonding b/w nearby segments
49
intrinsically disordered segments
flexible segments b/w rigid structures
50
Disulfide bond usage
sturdier bonds for extracellular use (uses cysteine side chains, which have sulfur in em)
51
what holds together each of the protein organizations?
1' -- covalent bonds 2' -- hydrogen bonds 3' -- weak noncovalent bonds and sidechain interactions 4' -- (same as 3')
52
antibodies;
proteins that bind to specific antigens, their binding sites are intrinsically disordered sequences, the 'variable domain'
53
antigen
the spp molecule an antibody binds to
54
epitope
the spp part of an antigen recognized by the antibody
55
what does antibody binding to an antigen do?
neutralizes it and marks it for destruction
56
what makes antibodies?
B lymphocyte
57
antigen structure
Quaternary structure that is Y shaped, with two heavy and 2 light chains, stabilized by disulfide bonds
58
Michaelis constant
Km; substrate whose enzyme is functioning at 1/2 Vmax
59
Lysozyme
it cuts polysaccharides in bacterial cell walls; its in our saliva tears and egg whites. 129a.a. // it hydrolyzes b/w sugars and can hold up to 6 polysaccharides at a time
60
enzyme process (4 steps)
substrate + enzyme, Enzyme-substrate complex, enzyme-product complex, enzyme + product
61
how does lysozyme break polysaccharides? (basic)
when the polysaccharide is in the right conformation, water Hydrolyzes it without energy use because it is energetically favorable.
62
Cofactor
additional molecules needed for functionm (hemoglobin subunits have a *heme group)
63
Coenzyme
organic cofactor, activated carrier that transports functional groups (ex. ATP has a phosphorous group)
64
how does lysozyme break polysaccharides? (advanced)
1) 6 sugars bind in active site and hydrolyzing happens D & E 2) ENZYME-SUBSTRATE COMPLEX, gLU35 GIVES AN ELECTRON via hydrogen, Asp52 can bind to C1 on D (malforms sugar) 3) sugar is now in a transition state where it can be broken Asp52 is covalently bonded to D 4) enzyme-product complex formed H2o splits H+ to Glu35 Asp52 bond displaces 5) product released
65
What are all vitamins?
coenzymes
66
Nucleic acids are what?
polypeptides of nucleotides, and it is one DNA molecule.
67
Allosteric enzymes...
have 2+ binding/active sites (active is for enzymes), Binding in one site normally causes a conformational change, which changes function
68
nucleosome parts
nucleosome core particle + linker DNA
69
nucleosome core particle parts
8 histones and about 146-147 bp of DNA & linker DNA (string b/w beads)
70
name of histones that bundle nucleosomes
H1 Linker histone
71
widths of all the chromatin levels of chromatin and names
nucleosomes; 11nm Chromatin fiber; 30nm Loop domains; 300nm 1 mitotic Chromosome; 700
72
2 different chromatin packing and unpacking techniques
ATP-dependent chromatin-remodeling complexes: Change the position of DNA wrapped around a nucleosome Histone-modifying enzymes; covalently modified histone tails (acetylation of lysine 9 turns heterochromatin on/off )
73
nucleotide parts
phosphate group, Ribose Sugar, R group (one of the 4 nitrogenous bases)
74
dNTP
deoxynucleotide triphosphate
75
purines and pyrimidines
purines are double ringed (A and T) pyrimidines are single rings (G and C)
76
how are nucleotides combined together?
covalent phosphodiester linkage
77
what holds together the two nucleic acids in a DNA helix
hydrogen bonding of complementary base pairing
78
which are stronger; A-T or G-C bonds?
G-C bonds
79
name all the proteins for DNA replications and which use ATP
s-s binding P helicase (ATP) topoisomerase ligase (ATP) Clamp loader (ATP) Sliding clamp DNA pol I and III Primase
80
how many catalytic domains does DNA pol III have and what is the purpose?
one is for replication and one is for proofreading; this lowers the error rate
81

Human Physiology + Cell and Molec Bio (8 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions