Quiz
Lecture Tutorial 1 Protein Structure and Function
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1Which of the following statements are TRUE
- AAlkane branches and benzene rings are non-polar
- BAlkane branches and benzene rings are polar
- CThe longer the branch, the more non-polar the amino acid
- DThe longer the branch, the more polar the amino acid
2Which of the following statements is FALSE
- A7/9 of the non-polar amino acids have only alkyl groups as a part of their side chain, methionine and tryptophan are exceptions to this
- B7/9 of the non-polar amino acids have only hydroxyl groups as a part of their side chain, methionine and tryptophan are exceptions to this
- CPolar, uncharged amino acids can become charged if pH changes
- DCysteine could be classes as either polar OR non-polar due to its S atom not carrying a lot of charge
3Which of the following is TRUE
- APolypeptide chains form via condensation reactions with water as a byproduct
- BPolypeptide chains form via elimination reactions with no byproduct being produced
- CAnother name for the peptide bond is the chi bond
- DThe only differences between amino acids are which way round the acid and amide groups are arranged
4Ω - [blank_start]omega[blank_end] - [blank_start]peptide bond[blank_end]
Ψ - [blank_start]psi[blank_end] - bond between [blank_start]carbons[blank_end]
ϕ - [blank_start]phi[blank_end] - bond between [blank_start]alpha carbon and nitrogen[blank_end]
χ - [blank_start]chi[blank_end] - bond between [blank_start]alpha carbon and side chain[blank_end]- Aomega
- Bpeptide bond
- Ccovalent bond
- Dcarbons
- Ealpha carbon and nitrogen
- Fcarbonyl carbon and nitrogen
- Galpha carbon and side chain
- Hcarbonyl carbon and side chain
- Ipsi
- Jphi
- Kchi
5Which of the following are TRUE
- AThere is no rotation between single bonds in polypeptide chains
- BSingle bonds in polypeptide chains can rotate +/- 180 degrees
- CPsi angle causes collisions between oxygens
- DPhi angles causes collisions between the hydrogens coming off of the nitrogen atom
- EPhi angle causes collisions between oxygens
- FPsi angles causes collisions between the hydrogens coming off of the nitrogen atom
6Most living organisms contain amino acids in their D configuration apart from some bacteria which can synthesise L enantiomers
- ARichtig
- BFalsch
7By definition, a trans peptide bond is [blank_start]180[blank_end] degrees, where as a cis peptide bond is [blank_start]0[blank_end] degrees. The peptide bond is [blank_start]linear[blank_end], [blank_start]flat[blank_end] and [blank_start]rigid[blank_end], meaning it [blank_start]doesn't allow[blank_end] rotation.
- A180
- B0
- C360
- D0
- E180
- F360
- Glinear
- Hbent
- Iflat
- J3 dimensional
- Krigid
- Lflexible
- Mdoesn't allow
- Nallows
- Osometimes allows
8Which of the following is FALSE
- AThe direction of the amino acid is sometimes left to right
- BThe direction of the amino acid is determined by the order of alpha carbon to carbonyl carbon to nitrogen
- CThe direction of the amino acid is determined by the order of carbonyl carbon to alpha carbon to nitrogen
- DR chains and O groups alternate on the polypeptide chain in order to avoid steric hindrance
9The secondary structure of a protein is how the polypeptide chain folds determined by [blank_start]phi[blank_end] and [blank_start]psi[blank_end] bonds, they are stabilised by [blank_start]hydrogen[blank_end] bonds.
- Aphi
- Bomega
- Cchi
- Dpsi
- Ephi
- Fomega
- Gchi
- Hhydrogen
- Iionic
- Jstrong covalent
10Which of the following are unfavourable amino acids for the formation of an alpha helix
- AProline - it is too bulky
- BGlycine - it is too flexible
- CHistidine - it is too bulky
- DTryptophan - it is too flexible
11In an alpha helix, the side chains point [blank_start]out[blank_end] so that there is a [blank_start]polar[blank_end] and non polar side. 1 turn is equal to [blank_start]3.6[blank_end] amino acids, or [blank_start]5.4[blank_end] Å. They are stabilised by [blank_start]hydrogen[blank_end] bonds between the o[blank_start]xygen[blank_end]s and h[blank_start]ydrogen[blank_end]s between the [blank_start]n[blank_end] and [blank_start]n+4[blank_end] amino acids.
- Aout
- Bpolar
- C3.6
- D5.4
- Ehydrogen
- Fxygen
- Gydrogen
- Hn
- In+4
12Beta pleated sheets are a type of secondary structure made up of multiple different polypeptide chains
- ARichtig
- BFalsch
13Beta Pleated Sheets usually consist of [blank_start]2-10[blank_end] sheets each made up of about [blank_start]6[blank_end] amino acids. They are joined by l[blank_start]oops[blank_end], c[blank_start]oils[blank_end] or t[blank_start]urns[blank_end] and stabilised by [blank_start]hydrogen[blank_end] bonds. Beta Pleated sheets can either be [blank_start]parallel[blank_end] where the polypeptide chains run in the [blank_start]same[blank_end] direction (with hydrogen bonds in a zig zag pattern) or [blank_start]antiparallel[blank_end] where the polypeptide chains run in [blank_start]opposite[blank_end] directions (with hydrogen bonds with a more parallel pattern). Sheets tend to have a [blank_start]right[blank_end] hand twist
- A2-10
- B6
- Coops
- Doils
- Eurns
- Fhydrogen
- Gparallel
- Hsame
- Iantiparallel
- Jopposite
- Kright
14Primary - [blank_start]order of amino acids[blank_end]
Secondary structure - how the polypeptide chain [blank_start]folds[blank_end] stabilised by [blank_start]hydrogen[blank_end] bonds between [blank_start]backbone[blank_end] [blank_start]peptide[blank_end] groups
Super secondary structure - different [blank_start]secondary[blank_end] structures put together
Tertiary structure - collection of [blank_start]secondary structures[blank_end] that fold to form a [blank_start]3D[blank_end] structure with a specific [blank_start]function[blank_end]
Quaternary structure - 2 or more [blank_start]tertiary[blank_end] structures put together to form a [blank_start]multi subunit protein[blank_end]- Afolds
- Border of amino acids
- Chydrogen
- Dcovalent
- Ebackbone
- Fpeptide
- Gpolypeptide
- Hsecondary
- Iprimary
- Jsecondary structures
- K3D
- L2D
- Mfunction
- Ntertiary
- Omulti subunit protein
- Psingular subunit protein
15[blank_start]Motif[blank_end] - a common secondary structure
[blank_start]Domain[blank_end] - secondary structures within a protein that have a function
[blank_start]Family[blank_end] - proteins with a similar structure but a different amino acid sequence and therefore function- AMotif
- BDomain
- CFamily
16Which of the following is INCORRECT
- AProtein folding can be facilitated by chaperones or chaperonins
- BProtein folding is non-random and dictated by the initial order of amino acids
- CProtein folding occurs via a process known as nucleation
- DProtein folding occurs via hydrolisis with water being a byproduct
17Which of the following is CORRECT
- ADisulfide bridges commonly form between cysteine and is a type of strong covalent bond
- BDisulfide bridges are week bonds that form between side chains of most amino acids
- CThere are 4 types of strong covalent bonds in tertiary structures
- DMetal ion co-ordination is a strong bond that forms between amino acid side chains in tertiary structutres
18Which of the following is CORRECT
- AQuaternary structures are formed by multiple different polypeptide chains
- BTertiary structures are formed by multiple different polypeptide chains
- CQuaternary structures are held together with strong, covalent bonds
- DQuaternary structures are held together with weak, covalent bonds
19Which of the following is CORRECT concerning protein folding
- ADriven by hydrophobic interactions
- BDriven by ionic interactions between amino acid side chains
- CFacilitated by the omega/peptide bond between amino acids in the polypeptide chain
- DDriven by interactions between different polypeptide chains in a protein
20Which of the following is INCORRECT
- AProtein folding can occur by itself with simple polypeptide chains
- BProtein folding can be facilitated by a chaperone where a helper protein guides and prevents incorrect folding without the use of ATP
- CProtein folding can be facilitated by a chaperonin where a helper protein guides and prevents incorrect folding without the use of ATP
- DProtein folding can be facilitated by a chaperonin where protein folding occurs within a larger protein structure using ATP
21Protein folding occurs via the formation of secondary structures via [blank_start]nucleation[blank_end]. These [blank_start]nuclei[blank_end] then come together to form domains, which then come together to form the almost final 3D tertiary structure. [blank_start]Conformational[blank_end] changes then tweak this structure to form the final, [blank_start]native[blank_end] 3D tertiary structure.
- Anucleation
- Bnuclei
- CConformational
- Dnative
22What did the Anfinsen experiment prove
- AThat proteins can be denatured (unfolded) by changes in pH or heat
- BAll information required for a protein to fold correctly is contained within its initial order of amino acids
- COnce a protein has been denatured it can not fold back to its original tertiary structure
- DProteins are adaptable to their environment
Informationen
- Beschreibung
- Medicine (BIOC 192) Quiz am Lecture Tutorial 1 Protein Structure and Function, erstellt von Eva Bonning am 04/09/2017.
- Autor
- Eva Bonning
- Sprache
- English
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