Quiz
Protein Structure
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Questions in this quiz (13)
1In what synthesis is a peptide bond formed?
- ADehydration
- BAddition
- CRedox
- DSubstitution
2The peptide bond is a single bond but its properties resemble that of a [blank_start]double bond[blank_end]. It is [blank_start]shorter[blank_end] than an expected C-N bond would be meaning that it is [blank_start]rigid[blank_end]. This means that there is no [blank_start]rotation[blank_end] about the bond. [blank_start]Steric interference[blank_end] between the groups means there is a [blank_start]trans[blank_end] arrangement around the bond. The partial [blank_start]negative[blank_end] charge on oxygen and partial [blank_start]positive[blank_end] charge on hydrogen in the amine group facilitates formation of [blank_start]hydrogen[blank_end] bonds with other molecules.
- Adouble bond
- Bshorter
- Crigid
- Drotation
- ESteric interference
- Ftrans
- Gnegative
- Hpositive
- Ihydrogen
3Disulfide bridges form between Cys units
- ATrue
- BFalse
4Other covalent bonds that form in protein structures are...
- ADisulfide bridges
- BGlycosylation
- CPhosphorylation
- DMethylation
- EAcetylation
- FSalt bridges
- GHydrogen bonds
5The first amino acid in a peptide is at the...
- AN terminal
- BC terminal
6A-helices are formed by [blank_start]hydrogen bonds[blank_end] between residues in the [blank_start]same[blank_end] polypeptide chain. The C=O and N-H of every [blank_start]4th[blank_end] peptide are involved in hydrogen bonding. This forms a regular [blank_start]right-handed[blank_end] helix. There are [blank_start]3.6[blank_end] residues per turn and the R groups lie on the [blank_start]outside[blank_end] of the helix.
- Ahydrogen bonds
- Bsame
- C4th
- Dright-handed
- E3.6
- Foutside
7B-pleated sheets are formed by the formation of hydrogen bonds between [blank_start]different[blank_end] [blank_start]linear[blank_end] polypeptide chains. The R groups lie alternatively above and [blank_start]below[blank_end] the place of the sheet. Proteins with high levels of B sheets are known as [blank_start]fibrillar[blank_end] and have more tensile strength with little [blank_start]elasticity[blank_end]. An antiparallel sheet describes the peptides running in [blank_start]opposite[blank_end] directions to one another. A parallel sheet describes the peptides running in the [blank_start]same[blank_end] directions as one another.
- Adifferent
- Blinear
- Cbelow
- Dfibrillar
- Eelasticity
- Fopposite
- Gsame
8What are the H bond donors? Check all that apply
- AOxygen in OH
- BNitrogen in NH
- COxygen in carbonyl
- DTriple covalently bonded N
9We can stabilise protein structures by forming [blank_start]disulfide bridges[blank_end] between cysteine subunits. [blank_start]Hydrogen bonding[blank_end] also occurs whereby 2 electronegative atoms compete for the same hydrogen atom. [blank_start]Hydrophobic[blank_end] regions in proteins also fold to minimise contact with the aqueous environment - residues within this region are unable to form [blank_start]hydrogen[blank_end] bonds. Electrostatic interactions occur between [blank_start]charged[blank_end] side chains. Van der Waals forces occur between molecules due to their [blank_start]spontaneous[blank_end] occurrence.
- Adisulfide bridges
- BHydrogen bonding
- CHydrophobic
- Dhydrogen
- Echarged
- Fspontaneous
10Van der Waals forces are the [blank_start]sum[blank_end] of all attractive or repulsive forces between molecules, not including covalent, hydrogen or [blank_start]electrostatic[blank_end] forces. They are based on small [blank_start]transitory[blank_end] dipoles occurring by chance within molecules. These arise due to the [blank_start]constant[blank_end] motion of electrons - at any point, one atom either side of a bond could be more [blank_start]electron dense[blank_end] than the other. This gives the atom a partial [blank_start]negative[blank_end] charge which can then induce a [blank_start]dipole[blank_end] in a neighbouring molecule.
- Asum
- Belectrostatic
- Ctransitory
- Dconstant
- Eelectron dense
- Fnegative
- Gdipole
11Proteins have several thousand possible structures. Only one of these structures will be functional.
- ATrue
- BFalse
12Creutzfeldt-Jakob disease, also known as [blank_start]Mad Cow Disease[blank_end], results in both [blank_start]neurological[blank_end] symptoms such as slurred speech and dizziness as well as psychology symptoms such as anxiety and hallucinations. It is caused by one form of prion protein, PrPSc, which can have two [blank_start]different[blank_end] structures despite their [blank_start]identical[blank_end] amino acid sequences. PrPc has an [blank_start]alpha-helical[blank_end] structure and is present in the normal [blank_start]cellular[blank_end] form. PrPSc, however, is [blank_start]insoluble[blank_end] and has a propensity to [blank_start]aggregate[blank_end]. The mixing of the misfolded protein with the cellular form triggers seeding whereby the pathogenic form causes the cellular form to [blank_start]misfold[blank_end].
- AMad Cow Disease
- Bneurological
- Cdifferent
- Didentical
- Ealpha-helical
- Fcellular
- Ginsoluble
- Haggregate
- Imisfold
13Sickle-cell anaemia is caused by a substitution of [blank_start]glutamate[blank_end] in normal haemoglobin for [blank_start]valine[blank_end] in mutated haemoglobin. Glutamate is [blank_start]negatively[blank_end] charged and hydrophilic whereas valine is aliphatic and [blank_start]hydropohic[blank_end]. This means that valine triggers a [blank_start]polymerisation[blank_end] of haemoglobins to remove themselves from the aqueous environment. This forms long aggregates of haemoglobin which distort the [blank_start]red blood cells[blank_end], causing anaemia.
- Avaline
- Bglutamate
- Cnegatively
- Dhydropohic
- Epolymerisation
- Fred blood cells
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- Description
- Cell Biology and Signalling Quiz on Protein Structure, created by Charlotte Jakes on 30/10/2019.
- Author
- Charlotte Jakes
- Language
- English
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