Exam 1 Flashcards

1
Q

Buffers

A

Large atoms that can accept/donate electrons

-Used to keep pH stable in a certain range

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2
Q

Zwitterion

A

Electrically nuetral atom, can have formal charges, but net charge is 0

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3
Q

Ampholyte

A

Acidic or Basic Groups present

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4
Q

Electrolyte

A

Free ions (passes charges)

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5
Q

Isoelectric Point (Pi)

A

pH where net charge is 0

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6
Q

Amino Acids more prevalent in L or D form?

A

L from (Rotates Left)

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7
Q

Sugars and nucleic acids more prevalent in which form?

A

D form (rotates right)

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8
Q

Essential AA

A

Body cannot produce and must be in diet

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9
Q

Non-essential AA

A

Can be produced by body

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10
Q

Myoglobin Structure

A

SIngle Polypeptide Chain

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11
Q

Hemoglobin Structure

A

Tetramer (32 alpha Helices)

-4 repeating myoglobin make up tetramer

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12
Q

Prostetic Group

A

Present per each strand in Mb and Hb used as an O2 binding site

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13
Q

Heme

A

Prostthetic group + protein

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14
Q

Central Atom in hemoglobin is?

A

Iron in Fe2+ state (ferrous)

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15
Q

Protopophyrin

A

Groups bonded to heme x4

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16
Q

Heme is planar or nonplanar when oxygenated

17
Q

What binds to O2 binding site when deoxyginated?

18
Q

allisteric effector

A

Something binds in one plane and effects another

19
Q

Pp Hb binds O2 at?

20
Q

Mb has higher affinity for O2 than Hb? T of F

21
Q

Bohr Effect

A

O2 is binded on a pH dependent curve

-the more acidic the blood (deoxygenated) lower Hb affinity for O2

22
Q

Examples of Allosteric Effectors

A

O2 binding
Bohr Effect (H+ binding)
2,3-biphosphoglyceride Binding

23
Q

Hb structure (in terms of dimers)

A

Two alpha/beta dimers

24
Q

T State of Hb

A

Tense State or Deoxygenated State

-Out of plane

25
R State of Hb
Relaxed State or Oxygenated State | -In plane molecule
26
T---> R Alterations
15 degree rotational change | Increased O2 affinity due to more O2 binding sites exposed
27
Carbonic Anahydrase
Enzyme that catolizes reaction of CO2 and H2O to H2CO3
28
What AA is replaced in Sickle Cell Anemia
GLU replaced with VAL | -Causes elongated Hb and creates Hb aggregates