Chapter 2: Basic Principles Flashcards

1
Q

Molecules of biological interest can be classifi ed into

A

ions, small molecules and macromolecules

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

Typical organic small molecules include

A

ligands of enzymes, substrates and effectors

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

Ions such as Ca 2+ play a key role in

A

signalling pathways

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

Biological

macromolecules are polymers which, by defi nition, consist of covalently linked

A

monomers

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

Three main factors determine the three-dimensional structure of a macromolecule

A
  1. dihedral torsional angles
  2. monomer interactions
  3. macromolecule and solvent
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

The solvent interactions can be categorised into two types

A

Solvation

hydrophobic interactions

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

The interactions between the building blocks of the macromolecule have two interactions types ____ and ____, which can be provided by (3 - H, ele, vn_)

A
  1. negative (to avoid atomic clashing)
  2. positive
  3. H-bonds - backbone main constitutive force and for residue-specific interactions
  4. electrostatic - opposite charges between residue side chains
  5. vdW - weak short-range force between all molecules thus responsible for the complementary surface if two molecules have highly complementary shapes.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

The allowable backbone angles provide a framework of

A

geometric constraints and a balance between attractive interactions and steric tension within the macromolecule.

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

The structural arrangement of groups of atoms is

A

conformation

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

The

angle describing the rotation around a bond between two atoms is called the

A

dihedral angle

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

conformational isomerism via interconversion giving individual isomers called

A

rotamers

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

How many dihedral angles does a nucleotide bonding situation have

A

3

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

the hydroxyl group in the anomeric position gives __ or __ symmetry in case of cyclic sugars in aquaous solution

A

cis or trans

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

Chairs conformers have bond angles close to

A

tetrahedral

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

Boat conformations for __-membered rings

A

6

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

Define primary structure

A

defi ned by the sequence of the amino acid residues, and is thus naturally dictated by the base sequence of the corresponding gene

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

Define 2nd structure

A

defines the localised folding of a polypeptide chain due to hydrogen bonding.

in its most basic form, to three different backbone conformations

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

Define super-secondary structure

A

specific combination of particular secondary structure elements giving structural motifs that can render a domain

19
Q

Define 3rd structure

A

defines the overall folding of a polypeptide chain of a grouping or domain.

20
Q

An individual polypeptide chain in an oligomeric protein is referred to as a ___

A

subunit

21
Q

The formation of oligomers is driven by ___ complementary between the individual monomers

A

shape

22
Q

Domain swapping is a fucntional ____ by oligomerisation

A

adaptation

23
Q

Which rwo macroscopic parameters does describe macromolecules?

A

Spatial extension

molecular mass

24
Q

We have two ways to describe spatial extension (flexibility)

A

end-to-end distance

radius of gyration

25
Q

end-to-end distance is useful for (which types of molecules?)

A

molecules with regular, mostly linear shape (e.g. rods), such as DNA molecules

26
Q

What does end-to-end distance describe?

A

average separation between the two ends of the molecule and depends on the molecular mass as well as the degree of flexibility. Entirely flexible molecules are called random coils and in such cases the end-to-end distance (now called h ) can be calculated by random walk statistics.

27
Q

Define:

  1. Radius of gyration
  2. Hydrodynamic radius
  3. Geometric radius
A
  1. used to estimate the physical extent of a macromolecule. One may visualise Rg for a given macromolecule by a hypothetical hard sphere centred at the centre of gravity of the molecule
  2. is based on the diffusional properties of the molecule in solution. Therefore, a hard sphere with radius R hydro is indicative of the apparent size of the dynamic solvated particle
  3. arises from rotation of the protein around its centre of gravity as a rigid body, the radius of gyration refl ects the variable (not necessarily spherical) shape of the molecule.
28
Q

What happens with DNA in its denatured form?

A

we get a single-stranded non-native form.

29
Q

Electrolytes that are weak are partially ____ bases or acids in aqueous solution., and for reagents their ____ ____ is dependent upon their ionization state at the environmental pH.

A

ionized

biochemical function

30
Q

the smaller the numerical value of pKa , the

____ the acid meaning its more ___, giving a weaker ___ ___

A

stronger
ionized
conjugate base

31
Q

Weak acids will be predominantly be ionised at ___ pH values

A

high

32
Q

weak bases will be predominantly be ionised at __ pH

A

low

33
Q

Polyprotic weak acids and bases are capable of donating or accepting more than one
____ ion

A

hydrogen

34
Q

Describe ionic strength!

A

govern the effect of counterion atmosphere for proteins due to the presence of charges residue side-chains.

So salt concentrations in a buffer can affect the soluability of proteins (and other charged biolofical species)

by increasing salt conc. –> salting out or salting in

35
Q

Describe:

  1. salting out
  2. salting in
A
  1. precipitation of the protein because not enough of waters to hydrate the charged residue side-chains.
  2. increased solubility because the charged residue side-chains are shielded therefore prevent aggregation
36
Q

Why is a buffer needed?

A

for electrolytes to resist change in pH in solution.

For weak electrlytes their ionic status varies with pH so we want to provide a constant environmental conditions during the cource of an experiment

37
Q

a buffer solution consists of an aqueous mixture of a:

A

aqueous mixture of a weak acid and its conjugate base

The conjugate base component will neutralise any hydrogen ions generated during an experiment whilst the unionised acid will neutralise any base generated

Buffers are most commonly used in the range 0.02–0.1 M

38
Q

What does the Henderson–Hasselbalch equation give?

A

pH estimation of a buffer solution, so idealy we want the pKa of bugger to be equal to pH in solvent. because the conjugate acid and conjugate base molecules are available in equal amounts and can thus neutralise added base or acid

39
Q

What is buffer capacity?

A

The ability of a buffer solution to resist a change in pH on the addition of strong acid or alkali.

In practice, Buffer Capacity is largest within the pH range of pH = p K a ± 1.

40
Q

Amino acids are ___ ____, meaning they can exist as bases and acid at the same time, thus giving cationic species at ___ pH and anionic species at ___ pH. And during a change in pH, Zwitterions (no charge intermediate species) is generated which is the predominantly form of amino acids in solution and crystalline state –> thus giving ___ properties

A

amphoteric substances
low
high
ionic

41
Q

Isoionic point: the pH at which ___ predominate in aquesous solution.

and similar too isoelectric point for _____

A

zwitterions

aminoacids

42
Q

the isoionic point is the pH at which the protein molecule possesses:

A

an equal number of positive and negative groups.

43
Q

the isoelectric point is the pH at which the protein is ____. _____

A

electrophoretically immobile

It is the pH at which, for example, the protein has minimum solubility. since it is the point at which there is the greatest opportunity for attraction between oppositely charged groups of neighbouring molecules and consequent aggregation and easy precipitation

44
Q

Below the isoelectric point the ___ and zwitterion will coexist in equilibrium in a ratio determined by the _____ equation

A

cation

Henderson–Hasselbalch