3-D Structure of Proteins Flashcards

(59 cards)

1
Q

What is the primary organization of proteins?

A

Amino acid sequence + disulfide bonds

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2
Q

What is the secondary organization of proteins?

A

Regular recurring arrangements of adjacent amino acids

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3
Q

What is the tertiary organization of proteins?

A

Arrangement of the total protein, the complete 3D structure

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4
Q

What is the quaternary organization of proteins?

A

The arrangement of multiple protein subunits

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5
Q

When a protein is denatured, what bonds aren’t broken?

A

Disulfide bonds

Peptide bonds

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6
Q

What is a domain, with regards to proteins?

A

A contiguous region with a distinct function

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7
Q

What are some examples of protein domains?

A

DNA binding
Transmembrane
Calcium binding

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8
Q

Peptide bonds and disulfide bonds are both which type of bond?

A

Covalent

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9
Q

Peptide bonds are ___ and ___.

A

Planar and rigid

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10
Q

Which amino acid acts as the “oxidative stress sensor”?

A

Cysteine

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11
Q

What are the 3 major secondary structure types in proteins?

A

Alpha helix
Beta pleated sheet
Beta turn

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12
Q

In alpha helices, where do the peptide bonds align?

A

Along the long axis

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13
Q

In alpha helices, where are the R groups?

A

Sticking out of the sides

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14
Q

Each turn in alpha helices uses about how many amino acids?

A

About 3.6

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15
Q

How are alpha helices stabilized?

A

Lots of hydrogen bonding

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16
Q

Which amino acid is generally a “helix breaker”?

A

Proline

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17
Q

What things are alpha helix destabilizers?

A
  • A string of several basic or acidic amino acids
  • A string of several amino acids with bulky side groups
  • Amino acids 3-4 residues apart which cannot interact
  • Proline residues
  • A string of glycine residues
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18
Q

How are beta pleated sheet chains arranged?

A

May be in parallel or anti-parallel fashion

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19
Q

What is beta pleated sheet?

A

Extended arrangement of polypeptides

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20
Q

What hold the adjacent chains together in beta pleated sheet?

A

Hydrogen bonds

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21
Q

Beta turns contain which amino acid?

A

Proline

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22
Q

In which conformation is proline found in beta turn?

A

The cis conformation

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23
Q

What converts proline from the trans to the cis conformation?

A

Proline isomerase

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24
Q

What are the two major groups of protein tertiary structure?

A

Globular

Fibrous

25
Are fibrous proteins primarily water soluble or insoluble?
Water insoluble
26
Which group of proteins (globular or fibrous) are structural proteins?
Fibrous proteins
27
How are fibrous proteins usually arranged?
In long chains or sheets
28
What are classic examples of right-handed alpha helix?
alpha and beta keratin
29
Where is alpha and beta keratin found?
Hair Nails Feather etc.
30
What type of amino acids are found in alpha and beta keratin?
Many hydrophobic amino acids
31
What is a protofilament?
2-stranded superhelix
32
How do alpha and beta keratin crosslink?
Via disulfide links
33
To create a perm, what bonds are broken and then reformed?
Disulfide bonds
34
How many types of keratin are there in the skin?
At least 18
35
Cytokeratins can be diagnostic for what?
Tumors
36
Most enzymes and protein hormones are what type of protein?
Globular proteins
37
Which structure is more complex in globular proteins than in fibrous proteins?
Secondary structure
38
What shape do globular proteins take on, due to the multiple arrangements of folding?
"spherical"
39
What are the 4 bond types found in the tertiary structure?
Hydrogen bonds Ionic bonds Hydrophobic interactions Van der Waals forces
40
What occurs in an H+ bond?
An electronegative atom (Usually O or N) acts as a Hydrogen acceptor
41
What is an ionic bond?
Attraction between oppositely charged atoms
42
What are hydrophobic interactions?
Forces that hold nonpolar regions together
43
What are van der Waals forces?
Weak attractions resulting from transient dipole formation
44
What proteins assist in folding or assembling subunits of a new protein?
Chaperone proteins
45
What are the most famous chaperone proteins?
Heat shock proteins
46
What causes prion diseases?
Improper folding of PrP protein
47
What is Scrapie?
Spongiform encephalitis found in sheep
48
What is kuru?
Human spongiform disease found in the Fore tribe of New Guinea
49
What is Creutzfeldt-Jacob disease?
Sporadic, hereditary degenerative neurologic disease
50
What causes cystic fibrosis?
Defective protein folding
51
Which protein is missing an amino acid leading to cystic fibrosis? Which amino acid is missing?
Chloride channel protein is missing Phe-508
52
When is quaternary structure found in proteins?
Only if the protein has more than one protein subunit
53
What are some huge proteins with quaternary structure?
Pyruvate dehydrogenase Ribosomes RNA polymerase
54
What is the best way to study protein structure?
Via x-ray crystallography
55
What things will denature the secondary-quaternary structure of proteins?
Heat pH extremes Detergents Organic solvents (alcohol, acetone, urea)
56
How can the primary protein structure be broken?
Boiling in a strong acid or base
57
What things can cleave proteins at specific dipeptide sites?
Proteases
58
What chemical can be used to reduce disulfide bonds?
Beta-Mercaptoethanol (BME)
59
Tertiary structure is dictated by what?
Primary structure