Nap Attack 6 Flashcards

1
Q

Anfinsen’s dogma

A

at least for small globular proteins, tertiary structure is determined exclusively by primary structure (based on study of addition and removal of mercaptoethanol)

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2
Q

native structure represents

A

a unique, stable and kinetically accessible minimum of the free energy

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3
Q

chemical interactions that stabilize polypeptides

A

covalent bonds, disulfide bonds, salt bridges, hydrogen bonds, long-range electrostatic interactions, Van der Waals interactions

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4
Q

How is stabilization from these weak bonds possible

A

strength in numbers, many weak bonds can make a large stable structure

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5
Q

Advantages of stabilization through weak interactions

A

allow for dynamic interactions and permit energy and information to more about the cell (pulling apart dna)

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6
Q

biological covalent bond strengths

A

200-460 kJ/mol (stable but can be broken under physiological conditions)

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7
Q

biological weak interactions strength

A

0.4-30 kJ/mol (continuously broken and reformed)

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8
Q

disulfide bond fun facts

A
  • proteins on the extracellular surface are no longer exposed to the reducing environment inside a cell
  • non-reducing environment disulfide bonds can form between the side chains of cysteine residues
  • found primarily in secreted extracellular proteins(eukaryotes)
  • uncommon in prokaryotes
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9
Q

four primary types of non-covalent forces that promote and stabilize protein structure

A
  • hydrogen bonds
  • electrostatic interactions(Ionic)
  • hydrophobic interactions
  • van der waals interactions
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10
Q

Second law of thermodynamics

A

the total entropy (disorder) of a system and it’s surroundings always increases in a spontaneous process

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11
Q

when a non polar molecule is introduced into water

A
  • a cavity is created
  • displaced water molecules reposition to form hydrogen bonds because there are less ways of forming hydrogen bond
  • decrease in entropy
  • non polars collect to release water molecules
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12
Q

The presence of other molecules in aqueous solution

A

disrupts the hydrogen-binding of water

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13
Q

when water surrounds a hydrophobic molecule

A
  • results in a highly structure shell, or solation layer, of water around the molecule (decreased entropy)
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14
Q

when non-polar groups cluster together

A

the extent of the solation layer decreases bc each group no presents its entire surface to the solution

  • less energy required to encage clumps of molecules than individually
  • favourable increase in entropy major thermodynamic driving force for association of hydrophobic groups in aqueous solutions
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15
Q

water is a

A

dynamic loose network of hydrogen bonds

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16
Q

hydrogen bond features in common with covalent and non-covalent bonds

A
  • charge-charge interaction using the partial positive charge on the hydrogen and negative charge on the electron pair
  • electron pair sharing between the hydrogen and the electron pair (reflected in bond length (in the middle of van der walls and covalent bond length)
17
Q

hydrogen bond

A

an electrostatic interaction between an electronegative atom with a hydrogen linked (donor) to another electronegative atom with a free electron pair (acceptor)

  • covalently bonded hydrogen atom, pair of non bonded electrons
  • highly directional (points directly at the electron acceptor pair
18
Q

most common hydrogen bond donors and acceptors (within biomolecules)

A

oxygen and nitrogen

19
Q

intramolecular hydrogen bonds

A

groups within the same molecule

20
Q

intermolecular hydrogen bonds

A

groups within other molecules

21
Q

significance of hydrogen bonding in biomolecular interactions

A
  • are a critical determinant of specificity
  • not a force of formation(could just bond with water)
  • little to be gained from a hydrogen bonding perspective with the formation of higher order structures
22
Q

the strength of a hydrogen bond depends on

A

its geometry

23
Q

polarizable

A

a molecule in which a dipole can be induced(from electric fields)

24
Q

induced dipole interactions

A

iteractions of polarizable molecules, shorter range than permanent dipole interactions

25
Q

fluctuations in the electronic charge distribution cause

A

molecules with neither a net charge nor permanent dipole moment to attract one another(happens if their close enough)

26
Q

when two molecules approach a very close distance

A

they synchronize their charge fluctuations so as to give a net attractive force (their surrounding electron clouds influence each other) ( their outer electron orbitals are overlapping and there is repulsion)

27
Q

van der waal attraction maximal when

A

two atoms are seperated by the sum of the van der Waal radii (theres a wall barring approach closer than distance rv)

28
Q

van der waals common in _____

A

core of protein, because of the close packing of hydrophobic side chains

29
Q

in a cell charges are surrounded by

A

dielectric medium that screens charges from one another

30
Q

E =

A

k* (q1*q2)/£r

31
Q

prion diseases

A

transmissible spongiform encephalopathies

- novel paradigm of infectious disease based on misfolding of self protein into a pathological, infectious conformation

32
Q

When a protein misfolds

A

new regions are surface exposed for antibody binding

- these misfolding dependent epitopes termed Disease-Specific epitopes (ideal vaccine targets)