Exam 1 Flashcards

1
Q

Which of the following have negative charges and which have positive charges?

a) ASPartate (D)
b) GLUtamate (E)
c) ARGinine (R)
d) LYSine (K)
e) HIStidine (H)

A

a) ASPartate (D) -
b) GLUtamate (E) -
c) ARGinine (R) +
d) LYSine (K) +
e) HIStidine (H) +

  • positively charged=basic=high pKr
  • negatively charged=acidic=low pKr
  • Histidine exception due to bohr effect*
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Amino acids are mostly ____ and sugars are mostly ____

a) D-
b) L-

A

Amino acids are mostly (L-) and sugars are mostly (D-)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Hif-1 signaling is induced by ____

A

hypoxia. In O2 rich environments, Hif-1 is ubiquinated (tagged for destruction). In O2 lacking environments, Hif-1 starts a cascade that upregulates Jun, Fos, AP1 then VEGF, glycolytic enzymes, and MMP’s

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

molecular weight =_____x_____

A

molecular weight = number of AA’s x 110

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

When the amino group is replaced by a carbonyl on the following amino acids it form an alpha-keto acid. Match the following amino acids with their correct alpha-keto acid:

a) alanine
b) aspartate
c) glutamate

1) oxaloacetate
2) alpha-keto-glutarate
3) pyruvate

A

a) alanine —- 3) pyruvate
b) aspartate —- 1) oxaloacetate
c) glutamate —- 2) alpha-keto-glutarate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

(T/F) Amino acids are the building blocks of protein. There are standard and non-standard amino acids. non-standard are NOT found in protein

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

(T/F) The relationship between K’eq and G in inversely proportional

A

true. also:
* (Delta)G (total)=G+G+G (additive)
* K’eq (total)=KxKxK (multiplicative)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

(T/F) When K’eq is positive, G is negative and the rxn proceeds fwd

A

true.

  • When K’eq is 1, G is zero, rxn is at equillibrium
  • When K’eq is negative, G is positive, and the rxn proceeds in reverse
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What do dehydrogenases do?

A

catalyze redox reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

(T/F) Proteins are built from the N-terminus to the COOH

A

False (build C to N) (breakdown N to C)

3 steps to the merrifield synthesis: 1-protection, activation, coupling

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Which one of the following is NOT a secondary protein structure?

a) alpha helix
b) beta turn
c) beta sheet
d) assembled subunits

A

d) assembled subunits (this is a quaternary structure)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Proteomics is a method used to compare the protein profiles between 2 different cells populations. What 2 methods are used to do this?

a) 2-D PAGE and ELISA
b) immunoblots and ELISA
c) 2-D PAGE and mass spectrometry
d) western blot and mass spectrometry

A

c) 2-D PAGE and mass spectrometry (2-D PAGE 1st uses electrophoresis to separate by charge then it separates by molecular weight)
* Immunoblots (western), ELISA, and immunocytochemistry are all use in ant-body/antigen interactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

(T/F) beta-turns contain proline in “cis” and require proline isomerase to convert it to “trans”

A

true. Most amino acids are in “trans” and are only in “cis” conformation when making a turn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Which one of the following is NOT a disease caused by a prion?

a) scrapie
b) Mad cow disease
c) Prader-willi syndrome
d) Kuru
e) Creutz-feldt-jacob

A

c) Prader-willi syndrome (this is caused by a chromosome mutation, I will talk about it more in exam 4 flashcards)
* know all the prion disease tho*

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

The formation of a globular protein, like a lipid micelle,_____ entropy (disorder)

a) increases
b) decreases
c) does not alter

A

a) increases The natural formation of anything (no energy required) will always increase entropy (disorder). It is only when work is put into a system that entropy decreases.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

(T/F) In REDOX reactions, compounds will either oxidize or reduce. If one compound becomes oxidized it become more positive and is also called the reducing agent.

A

true.
*electron donating=reducing agent=gets oxidized=exergonic=loses energy=negative E=catabolic

*electron accepting=oxidizing agent=gets reduced=endergonic=requires energy=positive E=anabolic

17
Q

(T/F) enzymes lower activation energy

18
Q

Match the following:

1) competitive inhibition
2) non-competitive inhibition

a) Vmax is unchanged and Km is increased
b) Vmax is decreased and Km is unchanged

A

1) competitive inhibition — a) Vmax is unchanged and Km is increased
2) non-competitive inhibition — b) Vmax is decreased and Km is unchanged

19
Q

Myoglobin (Mb) has a ____ curve, Hemoglobin (Hb) has a ____ curve

a) sigmoidal
b) hyperbolic

A

Myoglobin (Mb) has a (hyperbolic) curve, Hemoglobin (Hb) has (sigmoidal) curve

20
Q

In a high acid environment there is a lower affinity for O2, which shifts the O2 curve to the right. This is called the _____ effect.

A

Bohr. *Remember CADET, face right. CO2, Acid, 2,3 DPG (aka 2,3 BPG), Exercise, Temperature. These 5 things lower the affinity of O2

21
Q

The active site of an enzyme is where the ____ binds. It is a _____ cleft on the surface of the enzyme.

A

substrate, hydrophobic

22
Q

(T/F) When the concentration of [S] is high, V0=Vmax. This is an example of zero order kinetics

A

True. Also, when [S] is low, V0=Vmax[S]/Km+[S], this is an example of 1st order kinetics

23
Q

What percentage of Hb is normally glycosylated by glucose in the blood stream?

a) 1-2%
b) 4-5%
c) 11-12%
d) 15-20%

A

b) 4-5% This has to do with A1C measurement of diabetes patients. Quantifying HbA1C is useful for assessing long term diabetic control of blood glucose. Uncontrolled diabetics pts can have greater than 11%.

24
Q

(T/F) In the Cori cycle, muscles take in lactate and convert it to glucose to store as glycogen

A

false. Muscles take in glucose to store as glycogen. When the muscle contracts, the glycogen is broken down into glucose then to lactate and ATP. The lactate travels thru the blood to the liver where it is converted back to glucose and then stored as glycogen. The liver will breakdown its glycogen and send out glucose when the body has low blood sugar.

25
Q

(T/F) A deficiency of fructokinase or galactokinase is ok, however, a deficiency in fructose-1-phosphate aldolase or in galactose-1-phosphate uridyltransferase are both severe

A

true. a deficiency in fructose-1-phosphate aldolase causes hepatomegaly and a deficiency in galactose-1-phosphate uridyltransferase causes GALT

26
Q

If lactate is the main source of carbon___ is shuttled out. IF alanine is the main source of carbon then ____ is shuttled out

A

PEP, Malate (lactate:PEP) (alanine: malate) *remember which 2 go together

27
Q

(T/F) muscles have epinephrine receptors but not glucagon receptors

28
Q

Which one of the following is NOT a mitochondrial transporter?

a) pyruvate
b) PEP
c) malate
d) Oxaloacetate

A

d) Oxaloacetate

29
Q

(T/F) Sucrose is a non-reducing disaccharide

30
Q

(T/F) Glucose and Fructose are constitutional isomers

31
Q

(T/F) Sickle cell anemia (HbS) is an E6V (GLU to VAL) substitution on the hemoglobin beta chain

32
Q

(T/F) HbM is a condition where methemoglobin is bound to hemoglobin which causes FE2+ to oxidize to FE3+. FE3+ (Ferric) no longer binds to O2, resulting in cyanosis. Patients are treated with reducing agents, such as ascorbic acid or methylene blue

33
Q

An increase in serum amylase indicates____ damage
An increase in serum alkaline phosphotase indiactes _____damage.
An increase in aspartate or alanine transaminase serum levels indicate_____damage

A
  • increased amylase—pancreas damage
  • increase in alkaline phosphotase —bone tissue (bone cancer)
  • increase in aspartate or alanine transaminase —liver damage or MI (myocardial infacrtion)
34
Q

(T/F) Amino acids with bulky side groups are considered alpha helix stabilizers

A

false, they are destabilzers

35
Q

(T/F) Living organisms are “open” systems

A

true because we exchange energy and material with our surroundings