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Protein Structure

Charlotte Jakes 13 preguntas

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Preguntas del test (13)

  1. 1In what synthesis is a peptide bond formed?
    1. ADehydration
    2. BAddition
    3. CRedox
    4. DSubstitution
  2. 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.
    1. Adouble bond
    2. Bshorter
    3. Crigid
    4. Drotation
    5. ESteric interference
    6. Ftrans
    7. Gnegative
    8. Hpositive
    9. Ihydrogen
  3. 3Disulfide bridges form between Cys units
    1. AVerdadero
    2. BFalso
  4. 4Other covalent bonds that form in protein structures are...
    1. ADisulfide bridges
    2. BGlycosylation
    3. CPhosphorylation
    4. DMethylation
    5. EAcetylation
    6. FSalt bridges
    7. GHydrogen bonds
  5. 5The first amino acid in a peptide is at the...
    1. AN terminal
    2. BC terminal
  6. 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.
    1. Ahydrogen bonds
    2. Bsame
    3. C4th
    4. Dright-handed
    5. E3.6
    6. Foutside
  7. 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.
    1. Adifferent
    2. Blinear
    3. Cbelow
    4. Dfibrillar
    5. Eelasticity
    6. Fopposite
    7. Gsame
  8. 8What are the H bond donors? Check all that apply
    1. AOxygen in OH
    2. BNitrogen in NH
    3. COxygen in carbonyl
    4. DTriple covalently bonded N
  9. 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.
    1. Adisulfide bridges
    2. BHydrogen bonding
    3. CHydrophobic
    4. Dhydrogen
    5. Echarged
    6. Fspontaneous
  10. 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.
    1. Asum
    2. Belectrostatic
    3. Ctransitory
    4. Dconstant
    5. Eelectron dense
    6. Fnegative
    7. Gdipole

Información

Descripción
Cell Biology and Signalling Test sobre Protein Structure, creado por Charlotte Jakes el 30/10/2019.
Idioma
English
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