Lecture 4: solving protein structures Flashcards

1
Q

X-ray crystallography [pros & cons]

A
  • not limited by protein size
  • capable of very high-res structures
    //
  • requires protein crystals
  • normally only “sees” a single conformation
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2
Q

NMR [pros & cons]

A
  • captures multiple conformations
  • captures weak protein-protein or protein-ligand information
  • no need for crystals
    //
  • needs isotope labeling
  • limited by protein size [good for small proteins]
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3
Q

Cryogenic electronic microscopy (cryo-EM) [pros & cons]

A
  • works well for large complexes
  • no need for crystals
    //
  • does not work well for small proteins
  • limited by resolution structures [low res.]
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4
Q

Protein structure prediction [pros & cons]

A
  • no lab-bench work needed
  • can be done quickly
    //
  • limited by the size of the database
  • model still needs validation by empirical data
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5
Q

most commonly used method for protein structure identification

A

x-ray

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