Amino Acids, Peptides, and Protein Structures Flashcards

1
Q

Specific structure of protein is required for

A

Presenting a binding site

Creating an active site

Forming a special shape

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2
Q

What is Anfinsen’s experiment?

A

Native 3D protein –> added urea to denature protein and break sulfide bonds –> protein returns to primary sequence –> Remove urea –> protein refolds back to native structure

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3
Q

What did Alfinsen’s experiment imply?

A

Native structure is determined by:

1) sequence (primary structure)
2) Physical and chemical properties of amino acids

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4
Q

What are the nonpolar amino acids?

A

Alanine

Glycine

Valine

Leucine

Isoleucine

Phenylalanine

Tryptophan

Methionine

Proline

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5
Q

What force allows peptides to acquire an initial shape?

A

Hydrophobic effect

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6
Q

In soluble proteins, where are the polar and non-polar amino acids located?

A

Nonpolar are located in the interior

Polar are located on the surface

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7
Q

In membrane proteins, where are polar and non-polar amino acids located?

A

Nonpolar are clutered on the surface of the membrane protein (i.e. in the part that spans the membrane)

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8
Q

Which amino acid forms sulfide bonds

A

Cysteine

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9
Q

What are the uncharged, polar amino acids?

A

Asparagine

Serine

Threonine

Glutamine

Tyrosine

Cysteine

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10
Q

Which amino acids have hydroxyl groups that can form a H-bond

A

Serine

Threonine

Tyrosine

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11
Q

Which amino acids have carbonyl and amide groups that can form hydrogen bonds?

A

Asparagine

Glutamine

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12
Q

Which amino acid forms a physiolgoical buffer?

A

Histidine

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13
Q

Basic amino acids carry a __ change, acidic ones carry a __ charge

A

Basic = positive charge

Acidic = negative charge

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14
Q

Peptide bonds are created by __ reactions

A

Condensation

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15
Q

Change from primary to tertiary structure leads to a __ in free energy and is ___

A

Decrease in free energy = spontaneous reaction

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16
Q

Alpha helix is formed by

A

Hydrogen bonds between peptide-bond carbonyl oxygens and amides

17
Q

In alpha helix, H bonding occurs between

A

O of carboxy terminus of peptide 1 and H of amino terminus of peptide 5 (n+4)

18
Q

Where are the side chains in an alpha helix?

A

On the outside

19
Q

What two things can disrupt an alpha helix?

A

Proline

Positively charged amino acids

20
Q

Beta sheets are stabilized by

A

H bonds formed between peptide stands

21
Q

Beta bend requires __ amino acids, including

A

4 amino acids, including

Proline and glycine

22
Q

What is the function of proline in a beta bend?

A

Forces residue 2 to turn

23
Q

What is the function of glycine in a beta bend?

A

Allows steric freedom so residue 3 can form a H bond with residue 1

24
Q

What is Leinthal’s paradox?

A

If protein folding is simply a process of random residue-pairing, it would require a long time

25
What does the formation of secondary structure do?
Greatly reduces the number of possible combinations
26
What are protein motifs?
Super-secondary structural patterns
27
What is the significance of protein motifs?
Makes tertiary folding easier because it decreases residue combinations
28
At what stage do you see the connection of structure and function of proteins?
Secondary structure (super secondary structural patterns)
29
What is the function of alpha-alpha helix motif (aka Helix-loop-helix)
Transcription factors Channels
30
What is the function of beta-alpha-beta motif
Ligand binding
31
What is the function of beta-meander motif
protein-protein interaction
32
What is the function of the beta-barrel motif
Transporters
33
Domains are built from
Combination of motifs
34
What are the fundamental functional and 3D structural units of proteins
Domains
35
Peptide folding within a domain usually occurs ___ of folding in other domains
Independently
36
What does tertiary folding involve?
Folding of domains and function Turns loose, domain-formed peptide into a compact, high density protein by rearranging the positions of the domains
37
What interactions are invovled in teritary folding?
Covalent and non-covalent bonds
38
Types of bonds from strongest to weakest
Covalent (disulfide bond) Ionic H-bonds Hydrophobic interactions Van der Waals