biochem exam 1 Flashcards

1
Q

G=H-TS

A
  • g represents free energy change
  • h is the change in enthalpy
  • s is the change in entropy or randomness
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2
Q

dipole

A

between uncharged molecules

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3
Q

van der Waals

A
  • determines steric complementarity
  • stabilize macromolecules
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4
Q

f= (Q1Q2)/Er^2

A

force of ionic interaction depends on magnitude of charges, distance between charged groups and dielectric constant.

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5
Q

colligative property

A
  • bpt, mpt, osmolarity
  • don’t depend on nature of solute concentration
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6
Q

non colligative property

A
  • viscosity, surface tension, taste, color
  • depend on chemical nature of solute
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7
Q

chromatography

A

protein separation which protein remains fully folded

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8
Q

column chromatography

A

-separation using liquid phase
- proteins with Lowe affinity for solid wash off first

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9
Q

cation exchange

A

thing that binds column is cation and gets exchanged making column negative

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10
Q

size exclusion chromatography

A

big thing comes off first

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11
Q

affinity chromatography

A

protein with no affinity falls through column

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12
Q

SDS page

A
  • separates proteins by molecular weight
  • small at top large at bottom
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13
Q

ednan sequencing

A

identify amino terminal residue of polypeptide

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14
Q

ESI-MS

A

Identify peptides based on mass and charge

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15
Q

alpha helix

A

stabilized by hydrogen bonds between nearby residues

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16
Q

beta sheet

A

stabilized by hydrogen bonds between adjacent segments

17
Q

silk fibroin

A
  • antiparallel beta sheet
  • stronger than steel
  • very stretchy
18
Q

x ray crystallography

A

pro- no size limit, well established
cons- difficult for membrane proteins, can’t see hydrogens

19
Q

ligand

A

binds to a protein

20
Q

NMR

A

pros- no crystallization, can see hydrogens
cons- difficult for insoluble proteins, best with small proteins