Lecture 01 Flashcards

(37 cards)

1
Q

Name examples of protein functions

A

Catalysis
Transport
Structure
Motion
Communication

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2
Q

What is the one unifying concept about proteins regardless of their function?

A

Prior to any action taken by the protein a ligand must bind to it to signal a change

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3
Q

What is the pH range of blood?

A

7.35 - 7.45

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4
Q

What is a buffer?

A

Mixture of weak acid and conjugate base that provides a reservoir of proton-accepting and proton-donating species.

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5
Q

Why are buffers important?

A

Maintains pH of body systems at the appropriate range

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6
Q

When are buffer solutions most effective?

A

When the pH is equal to the pKa of the acid, but it can remain 1 unit above or below the pKa

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7
Q

How do you find the buffering range?

A

Add and subtract 1 to the pKa; this is also the region where the titration curve is less steep

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8
Q

pH < pKa

A

Protonated/acidic form dominates

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9
Q

pH > pKa

A

Deprotonated/basic form predominates

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10
Q

Name the major buffer systems of the human body

A

Proteins, phosphate, and carbon dioxide/bicarbonate

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11
Q

Phosphate pKa2 is within the effective range of physiological pH (7.2)

A

6.8

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12
Q

Bicarbonate buffer pKa

A

6.1

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13
Q

Which buffer system is the only one regulated by physiological processes?

A

Bicarbonate

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14
Q

What organ regulates carbon dioxide (CO2) levels?

A

Lungs

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15
Q

What organ regulates bicarbonate (HCO3-) levels?

A

Kidneys

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16
Q

Why does dissolved CO2 represent acid concentration?

A

Carbon dioxide forms carbonic acid but carbonic acid is not stable in aqueous solution

17
Q

Define dissolved CO2

A

Partial pressure of CO2 x solubility coefficient (alpha)

18
Q

Which amino acid is not chiral?

19
Q

Which stereoisomer is physiologically relevant for the chiral amino acids?

20
Q

Why are the hydroxy groups of Ser, Thr, and Try significant?

A

They are potential sites of protein phosphorylation

21
Q

What is significant about the hydroxy groups of Ser and Thr, not Tyr?

A

They are targets of O-linked glycosylation

22
Q

What is significant about the amide nitrogen of Asn?

A

It is the target of N-linked glycosylation

23
Q

What is significant about the R groups of Tyr and Cys?

A

They are ionizable; Tyr is also aromatic

24
Q

Which amino acids are acidic and carry a full negative charge at pH 7.2?

25
Which amino acids are basic and carry a full positive charge at pH 7.2?
Arg and Lys
26
Which amino acid is basic but carries a partial positive charge?
His
27
pKa ranges of alpha-carboxyl groups
2.2 - 2.8
28
pKa ranges of alpha-amino groups
8.5 - 9.5
29
Why is the pKa value of an amino acid R group in water not accurate when that amino acid is part of a protein?
Electrostatic interactions with other atoms in the proteins can increase or decrease its affinity for protons
30
What amino acid is commonly found in the ligans binding sites of proteins?
His
31
What is the pKa range of histidine side-chains in different proteins?
4 - 9; 5.0 - 8.0 frequently seen
32
Define isoelectric point (pI)
pH at which an amino acid has a net charge of zero.
33
What is true of an amino acid at its pI?
It is least solule in water and does not migrate in an electric field.
34
How to calculate pI
If there is no ionizable side chain, take the average of the two pKas. If there is an ionizable side chain, locate the species with no net charge and use the pKa values on either side of it.
35
What are the two torsional angles that define secondary structure of proteins?
Phi: alpha-carbon and alpha-amino Psi: alpha-carbon and alpha-carboxyl
36
Why is a Ramachandran Plot important?
It reports on the compatibility of all possible combinations of the two torsion angles with respect to protein structure.
37
What did the Ramachandran Plot demonstrate?
Steric hindrance caused by R groups limits the tolerated combinations of phi and psi angles.