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Conformational Changes in Proteins

Kirstin Latimer Cells Prelims Inglés 13 fichas

Fichas del conjunto (13)

  1. 1What does binding of an ion or metabolite involve?- non-covalent interactions
    - stereoselectivity
    - conformational changes
  2. 2What is key to cellular activity?- molecular recognition
    - successful binding
  3. 3What is the function of induced fit? Give an example.- substrate strain
    - supports catalysis
    - allows conformational adjustment
    - forms favourable micro-environment
    - excludes unfavourable molecules
    - glucose --> glucose-6-phosphate
  4. 4What is the role of allosteric regulation? Give an example.- often multimeric
    - binding at one site alters the binding of the substrate to the active site
    - primes enzyme to be active/inactive
    - e.g. inhibition of PFK by ATP and citrate
  5. 5What are the two methods for determining protein structure?- NMR
    - X-ray diffraction
  6. 6Describe the use of NMR.- in solution, aqueous phase
    - good for globular proteins
    - assesses conformational flexibility
    - detects interactions between magnetic isotopes with an applied magnetic field
  7. 7Describe the use of X-ray diffraction.- solid state
    - for fibrous and globular proteins
    - generates structures at atomic resolution for molecules that form regular crystals
    - comparing active and inactive states
    - X-rays scattered by electrons in crystals = e density map = distribution of atoms
  8. 8What is the relationship between theta and [L] for a protein with a single binding site? Define theta and [L] and give an example.- theta = fraction of sites occupied by L
    - L = ligand
    - if Kd is high, theta is low = less stability
    - relationship predicts a hyperbolic curve
    - interaction of P and L is independent of [L]
    - e.g. myoglobin
  9. 9What is the relationship between theta and [L] for a multimeric protein? Give an example.- relationship fails
    - sigmoidal curve
    - cooperativity in the binding curve
    - e.g. oxygen binding to haemoglobin
    - oxygen affinity increases as pO2 increases
    - due to allosteric effects
    - concerted model
  10. 10Describe the concerted model of cooperativity.- each subunit has 2 conformations
    - tense = inactive, low affinity for substrate, strong interaction with other subunits
    - relaxed = opposite
    - all subunits have to be in the same conformational state
  11. 11What cellular activities are conformational changes key to?- signalling
    - enzyme pathways
    - synthesis
  12. 12How are conformational changes important in signalling? Give an example.- mechanism for sensing the state of a cell + surroundings
    - hormone binding to receptors e.g. adrenaline binding to beta-adrenergic receptor
    - different subunits have different functions
  13. 13Describe the functions of the different subunits in signalling. Give an example.- regulatory = receive signal and transmit to the catalytic subunits by conformational changes
    - activation of cAMP-dependent protein kinase

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Prelims Cells Fichas sobre Conformational Changes in Proteins , creado por Kirstin Latimer el 06/01/2016.
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Kirstin Latimer
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