Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Foundation of Medicine > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

What is the basic structure of atoms

A

Nucleus with protons (+) and neutrons (No charge) Both mass=1
Electrons in outer ring (-) mass is negligible

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

What is the basic periodic table structure

A

Groups= Vertical (Shared chemical properties, increasing electron orbitals)
Periods= Horizontal rows (same number of electron shells, increasing from 1-7)

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

What is ionisation energy

A

Energy required for 1 mole of electrons to be discharged
Increases along periods
Decreases down groups

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

What is electron affinity

A

Energy released when electron is attached to neutral atom forming -‘ve ion
Increases along periods
Decreases down groups

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

What are the main types of bonds

A

Covalent (shared pair of electrons)
Ionic (opposite charges attract)
Hydrogen (H-O, H-F, H-N)
Van der Waals (non polar Pd-Pd & LDF’s)
Hydrophobic (Non polar & polar substance)

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

What shape do carbon molecules make

A

Tetrahedral as 4 bonds can be made- valency

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

What is electronegativity

A

Measures how strongly atoms attract bonding electrons
High number- more likely to attract electrons

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

What are common reactions of O2

A

Phosphorylation/dephosphorylation
Acylation
Carboxylation
Esterification

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

What is condensation reaction

A

2 small molecules join to make 1 large molecule and eliminate H2O

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

What is hydrolysis reaction

A

H2O is added to a large molecule to break it into 2 constituents

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

What are redox reactions

A

Transfer of electrons

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

What is oxidation and reduction

A

Oxidation is LOSS
Reduction is GAIN

as 1 is oxidised the other is reduced

Oxidising agent is reduced
Reducing agent is oxidised

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

What functional groups are common in biological molecules

A

Methyl groups
Amino groups
Carboxyl groups
Ester links
Carbonyl groups
Phosphates

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

What are some functions of biomolecules

A

Information storage (DNA)
Structure (Teeth, bone, cartilage)
Energy generation (Glycolysis, citric acid cycle electron transport chain)
Energy storage (ATP)
Specificity (Receptors, enzymes, hormones)

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

Major classes of biomolecules

A

Peptides (amino acids)
Proteins (amino acids)
Lipids (steroids, phospholipid)
Nucleic acids (DNA, RNA)
Carbohydrates (mon- ,di-, polysaccharides)

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

What is the 1st law of thermodynamics

A

Energy is neither created nor destroyed (in conversion of 1 energy form to another)

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

What is the 2nd law of thermodynamics

A

When energy is converted from one form to another, some energy become unavailable to do work

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

What is entropy (ΔS)

A

the randomness and disorder of a reaction

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

What is enthalpy (H)

A

Measurement of energy (heat content) in a given reaction
Change is also calculated (ΔH)

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

What is free energy change (ΔG)

A

The amount of energy released in the conversion of reactants to products under standard conditions

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

How is free energy change calculated

A

ΔG= (energy of products) - (energy of reactants)

ΔG= ΔH- TΔS

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

What is an exergonic reaction

A

Total free energy of product is LESS than that of reactant
(NEGATIVE ΔG so occurs spontaneously)

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

What is an endergonic reaction

A

Total free energy of the reaction product is GREATER than that of reactant
(POSITIVE ΔG so cannot occur spontaneously)

Input of energy needed to proceed

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

How is ΔG determined for a given reaction A + B→ C + D

A

ΔG = ΔGo’ + RTln([C][D]/[A][B])

R is universal gas constant (8.3JK-1mol-1)
T = absolute temperature (Kelvin)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Free energy change is always under standard conditions, What are these in the body?
T = 298 K 1 atmosphere pressure 1 M (1 mol/l) concentration of reactants (except for H+) pH = 7
26
How is ΔG related to equilibrium
The further towards completion the point of equilibrium is, the more free energy is released ΔG values near zero are characteristic of readily reversible reactions
27
What cellular processes are unfavourable for spontaneous reactions
having to proceed in +'ve ΔG direction transport against gradient synthesis of large molecules
28
What is ATP structure
- Less stable than ADP due to electrostatic repulsion of close negative charges on phosphates Phosphate groups linked by anhydride bonds(high energy) Which attach to a sugar and a base
29
What is metabolism
All reactions taking place in the body divided into 2 subsections
30
What are the 2 subsections of metabolism
Catabolism- Break down complex molecule into smaller ones releasing energy Anabolism- Synthesise complex molecules from smaller ones requiring energy
31
What can be used as a control point in metabolic pathways
Reactions with large negative ΔG values
32
What are characteristics of water
Polar- electrons shared unequally Forms a dipole Ionic + polar substances dissolve in it i.e hydrophilic Has hydrogen bonding between molecules
33
What happens when non-polar substances go into water
Solid types do not dissolve and liquids form 2 layer system as non-polar molecules are hydrophobic
34
What are amphipathic molecules
A molecule that is both hydrophilic and hydrophobic -Polar head and non-polar tail -Form micelles in water
35
how does amphipathic molecule- Sodium palmitate work
Is a fatty acid that's the sodium salt of palmitic acid- soap -Forms micelles with tails gathering at centre and heads protecting around
36
What groups do all amino acids contain
-Amino -NH2 -Carboxyl -COOH -Hydrogen -H -Side R group ALL ATTACHED TO CENTRAL C
37
What are stereoisomers
Non-superimposable mirror images All D- and L- forms of amino acids are stereoisomers
38
What are the types of amino acids
Basic (positively charged) Acidic (negatively charged) Polar (Hydrogen bonding) Hydrophobic (Hydrocarbons)
39
What are basic amino acid examples
Lysine Arginine Histidine
40
What are acidic amino acid examples
Aspartic acid Glutamic acid
41
What are polar amino acid examples
Glycine Serine Asparagine Glutamine Cysteine Tyrosine Threonine
42
What are hydrophobic amino acid examples
Leucine Proline Alanine Valine Methionine Tryptophan Phenylalanine Isoleucine
43
How do peptide bonds form
Two amino acids join by attraction of negatively charged COO- group and positively charged NH3+ group Eliminates H2O
44
What is the direction of a peptide
Runs from N-Terminal residue at 1 end to C-terminal residue at the other
45
What are the characteristics of peptide bonds
partial double bond character Planar structure strong and rigid- important in folding proteins
46
What are acids and bases in terms of protons
Acid molecules can donate a proton Bases accept protons
47
What does the strength of an acid depend upon and how is it calculated
How readily it can donate a proton (hydrogen ion) and is measure by acid dissociation constant Ka pKa= -log10[Ka]
48
What is pH and how is it calculated
The measurement of amount of proteins in a solution pH= -log10[H+]
49
What is a buffer
Solution used to control the pH of a reaction mixture
50
What are zwitterions
amino acids without charged side groups in a neutral solution -NO NET CHARGE -Gives buffering properties to proteins influencing function
51
What are the different protein structures
Primary Secondary Tertiary Quaternary
52
What is a primary protein
The sequence of amino acids in polypeptide
53
What is secondary structure
Localised conformation of the polypeptide backbone
54
What are the types of secondary proteins
Alpha helix Beta pleated sheet & strands Triple helix Some proteins have more than 1 of these elements
55
What is alpha helix
Rod like, with 1 polypeptide chain, spirals
56
What is a beta pleated sheet/strand
Backbone almost completely extended, can involve more than 1 chain Can run antiparallel or parallel with turns between strands -Also can be a repeated zig zag structure
57
What is a collagen triple helix structure
Triple helix- Three left-handed helical chains twisted around each other form a right-handed superhelix Influences strength of connective tissue, weakened collagen= bleeding gums
58
What is a tertiary protein
the three-dimensional structure of an entire polypeptide, including all its side chains Has fibrous and globular proteins
59
What are fibrous proteins
Have polypeptide chains organised approximately parallel along a single axis - consist of long fibers or large sheets - tend to be mechanically strong - are insoluble in water and dilute salt solutions - play important structural roles in nature
60
What are examples of fibrous proteins
Keratin of hair Wool Collagen of connective tissue of animals
61
What are globular proteins
Proteins which are folded to a more or less spherical shape - they tend to be soluble in water and salt solutions - most of their polar side chains are on the outside and interact with the aqueous environment by hydrogen bonding and ion-dipole interactions - most of their nonpolar side chains are buried inside - nearly all have substantial sections of alpha-helix and beta-sheet
62
What are examples of globular proteins
Myoglobin Haemoglobin
63
What forces stabilise tertiary structures
Covalent disulphide bonds Hydrophobic interactions Hydrogen bonds Electrostatic interactions-salt bridge
64
What do amino acid substitutions do to protein structure- sickle cell anemia example
Significant functional changes Single nucleotide change makes altered protein (Glutamic acid swapped for valine) Valine= Hydrophobic Glutamic acid= Acidic so low O2: haemoglobin polymerises blocking capillary blood flow
65
What causes denaturation of proteins
Heat Extreme pH change Detergents, urea Reducing agents
66
What is quaternary protein structure
the spatial arrangement of polypeptide chains in a protein with multiple subunits
67
what is a quaternary protein example
Haemoglobin -Has 4 subunits Each ahs a haem group binding to 1 O2 molecule Binding of 1 molecule changes the affinity at other subunits - allosteric regulation
68
What does haemoglobin do
Transports oxygen in the blood

Foundation of Medicine (23 decks)

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