Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Clinical Chemistry Lecture 2 > Proteins > Flashcards

Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Chemistry flashcards Periodic Table flashcards Chemistry 101 flashcards Organic Chemistry 101 flashcards
0
Q

What does primary structure determine?

A

1 identity of protein
2 molecular structure
3 functions performed
4 molecular binding

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

Analytic processes used in the laboratory

A

Chromatography
Electrophoresis
Dye binding
Light absorbance

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

Properties of secondary structure

A

Strength

Flexibility

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

3 structures of secondary structure

A

a-helix
B-pleated sheet
Bend conformations or turns

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

It refers to overall shape or conformation of the protein molecule (known as the fold)

A

Tertiary structure

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

Results from interaction of side chains

A

Tertiary structure

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

What does tertiary structure determine?

A

Function

Physical and chemical properties of protein

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

What stabilizes tertiary structure?

A

Hydrophobic effect
Ionic attraction
Hydrogen bonds
Disulfide

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

Shape from interaction of more than one protein molecule

A

Quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Forces that hold together quaternary structure

A

Non-covalent (H bonds, electrostatic interaction)

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

Lost of the native or naturally occurring folded structure

A

Denaturation

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

Denaturation can be accomplished by action of

A

Heat
Acid
Alkali
Enzymes

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

Contain peptide chains composed of only amino acids

A

Simple proteins

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

Functions of globular proteins

A

Transporters
Enzymes
Messengers

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

Characteristics of globular proteins

A

Symmetrical and soluble in water

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

Characteristics of fibrous proteins

A

Asymmetrical
Inert
With hydrophobic R groups

16
Q

Examples of globular protein

A

Albumin
Hemoglobin
Immunoglobulin

17
Q

Examples of fibrous protein

A

Troponin

Collagen

18
Q

What are conjugated proteins?

A

Proteins that consist of a protein and prosthetic group

19
Q

It defines the characteristics of the protein (conjugated protein)

A

Prosthetic group

20
Q

Examples of conjugated proteins

A

Metalloprotein
Lipoprotein
Glycoprotein
Nucleoprotein

21
Q

Examples of metalloproteins

A

Ferritin (iron)
Cerruloplasmin (copper)
Hemoglobin
Flavoprotein

22
Q

Examples of lipoprotein

A

HDL

LDL

23
Q

Examples of glycoprotein

A

Haptoglobin

a-antitrypsin

24
Q

Example of nucleoprotein

A

Chromatin

25
Q

What is the N content of serum proteins?

A

16%

26
Q

Other term for prealbumin

A

Transthyretin

27
Q

Characteristics and properties of protein

A

1 contain nitrogen atoms
2 can be positively or negatively charged
3 isoelectric point: number of positive = number of negative groups
4 (-) : pH>pI solution and (+) : pH<pI solution
5 solubility depends on the number and type of its amino acid and pH
6 molecular size : macromolecules with an average of 200-300 amino acids
7 synthesized in the liver (plasma proteins) and plasma cells (immunoglobulins)
8 catabolism : routes for converting proteins to free amino acids

28
Q

Control protein synthesis

A

Thyroxine
GH
Insulin
Testosterone

29
Q

Control protein catabolism

A

Glucagon

Cortisol

30
Q

Degrades extracellular and intracellular proteins

A

Lysosomal pathway

31
Q

Degrades extracellular proteins

A

Cytosolic pathway

32
Q

Remove nitrogens from AA

A

Transaminations

33
Q

Products of transamination

A

Ammonia

Ketoacids

34
Q

Oxidized and converted to glucose or fat

A

Ketoacids

35
Q

Converted to urea in hepatocytes and excreted in urine

A

Ammonia

Clinical Chemistry Lecture 2 (4 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions