Lecture 16 Flashcards

1
Q

what are the different types of globular proteins?

A
  1. catalysis- enzymes
  2. regulatory- hormones
  3. defense-antibodies
  4. transport in blood- albumin
  5. oxygen delivery- hemoglobin
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2
Q

What are the different kinds of structural proteins?

A
  1. extracellular matrix- collagen and elastin
  2. contractile- actin and myosin
  3. signal transduction-specific receptors
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3
Q

types of covalent bonds?

A

peptide and disulfide

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4
Q

types of non-covalent bonds?

A

hydrophobic interactions
hydrogen bonds
ionic bonds

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5
Q

What amino acids will participate in hydrophobic interactions?

A

valine, leucine, isoleucine, alanine

and phenylalanine

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6
Q

What do hydrogen bonds do during protein folding?

A

stabilize the secondary structures of a-helix and b-sheet
Hydrogen bonds between amino acid side chains
stabilize the tertiary structure of proteins

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7
Q

What is the purpose of chaperones or heat shock protiens?

A
  1. help fold proteins that do not fold by themselves
  2. bind to aggregated proteins
  3. unfold and refold misfolded proteins
  4. Direct proteins to degradation in proteasomes and lysosomes
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8
Q

What is the function of Hsp 70?

A

prevents the aggregation of unfolded protein.

It binds to hydrophobic regions of an extended
polypeptide and prevents premature folding of
a protein

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9
Q

What is the function of Hsp 60?

A

have a barrel shape and are required for correct folding of cellular proteins that do not fold spontaneously

Hsp 60 can be used to aid refolding of a protein after it has crossed a cellular membrane.

This needs ATP

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10
Q

Ubiquitin-Proteasome Complex

A

Misfolded or defective proteins are normally tagged
by the small protein ubiquitin and degraded in the
ubiquitin-proteasome system

ATP dependent

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11
Q

When does piron disease occur?

A

When the normal prp protein changes 3-D conformation due to changes in secondary structure

normal prp = more alpha helices

mutated prp = more beta sheets

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12
Q

Routes of transmission of piron disease?

A
  1. genetic
  2. ingestion of infected meat
  3. blood transfusion
  4. brain surgeries and procedures
  5. injection of infected human growth hormone
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13
Q

How can hydrogen bonds be broken?

A

high temperature, 5-10 M urea, or salt

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14
Q

how are hydrogen and ionic bonds broken?

A

strong acids or bases.

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15
Q

How are hydrophobic interactions broken?

A

1-2% of the detergent Sodium dodecyl sulfate (SDS)

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16
Q

How are disulfide bonds broken?

A

β-mercaptoethanol