Protein Primary Structure Flashcards

(26 cards)

1
Q

What is a peptide bond?

A

A bond formed between the a-carboxyl of one amino acid and the a-amino of another, with the removal of water

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2
Q

What are the phi (ɸ) and psi (Ѱ) angles?

A

Angles around the N-Cα and Cα-C bonds of amino acids that determine protein conformation

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3
Q

What does the Ramachandran plot represent?

A

Plots degrees of freedom of phi and psi angles on x (phi) and y (psi) axes

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4
Q

What do the red and yellow regions on a Ramachandran plot indicate?

A

Red region = conformations with no steric clashes; Yellow region = allowed regions with slight steric clashes

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5
Q

Why is glycine special in the context of the Ramachandran plot?

A

Glycine has a hydrogen R-group, allowing it to exist in any of the four quadrants of the plot

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6
Q

What are the main types of physiochemical interactions in proteins?

A
  • Hydrogen bonds
  • Hydrophobic interactions
  • Ionic interactions
  • Covalent bonds
  • Disulfide bridges
  • Van der Waals forces
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7
Q

What is the characteristic structure of an alpha-helix?

A

A spiral conformation where every backbone carbonyl oxygen forms a hydrogen bond with an amide group of an amino acid 4 residues ahead

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8
Q

How many amino acids are typically in one turn of an alpha-helix?

A

Approximately 3.6 amino acids

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9
Q

What defines a beta-strand?

A

A segment of 5-10 amino acids that rarely exists alone and usually aligns with other strands to form a sheet

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10
Q

What are loops in protein structure?

A

Flexible regions present on the surface of proteins, rich in polarity, and form hydrogen bonds with surrounding water molecules

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11
Q

What are domains in protein structure?

A

Tightly folded sub-regions of a polypeptide, often serving independent functions and comprised of structural motifs

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12
Q

What are the three categories of protein domains?

A
  • α-domain
  • β-domain
  • αβ-domain
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13
Q

What experimental approaches are used to determine tertiary structure?

A
  • X-ray crystallography
  • NMR
  • Cryo-EM
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14
Q

What is X-ray crystallography?

A

A technique that bombards protein crystals with electrons to amplify and detect/diffract the protein structure

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15
Q

What are the steps involved in crystallography?

A
  • Protein expression
  • Purification
  • Precipitation
  • Sample preparation
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16
Q

What factors affect protein solubility during crystallization?

A
  • Concentration
  • pH
  • Salts
  • Polar solvents
  • Temperature
17
Q

What are the two methods of crystallization?

A
  • Vapour diffusion
  • Dialysis method
18
Q

What is Bragg’s Law?

A

λ = 2dSinΘ, where λ is the wavelength, d is the Bragg plane separation distance, and Θ is the angle of incidence

19
Q

What is the purpose of AlphaFold?

A

To predict protein structure de novo using deep neural networks trained on specific properties

20
Q

What are the three overlapping problems of the protein folding problem?

A
  • The Folding code
  • Computational problem
  • Kinetic question
21
Q

What is the primary driving force behind protein evolution?

A

Gene duplications

22
Q

What is the role of divergence in protein evolution?

A

Further modifies existing paralogs, leading to more diversity between protein families

23
Q

What is phylogenetics?

A

The study of evolutionary history of species through construction and analysis of phylogenetic trees

24
Q

What are the two main tree building methods in phylogenetics?

A
  • Distance methods
  • Character-based methods
25
What is the significance of bootstrap analysis in phylogenetics?
A statistical technique to assess the reliability of phylogenetic trees
26
Fill in the blank: The three approaches to protein engineering are _______.
[Directed evolution, Semi-rational design, Rational design]