PROTEINS PT 1 Flashcards

1
Q

Greek word of Proteins

A

Proteus

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2
Q

stabilizing thick filament of your muscles

A

Titin

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3
Q

proteins in saliva

A

salivary amylase

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4
Q

building blocks of proteins

A

alpha amino acids

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5
Q

Alpha amino acids have a _____ carbon, except for ______

A

chiral, glycine

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6
Q

Oxytocin, the smallest known protein has how many amino acids?

A

9 AAs

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7
Q

Titin has how many amino acids?

A

25,000 AAs

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8
Q

Acidic Amino Acids examples

A

Aspartic Acid, Glutamine

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9
Q

They are negatively charged and release proton

A

Polar Acidic Amino Acids

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10
Q

positively charged at physiologic pH, accept proton

A

Polar Basic Amino Acids

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11
Q

3 examples of polar basic AAs

A

Histidine, Lysine, Arginine

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12
Q

cannot be synthesized by the body, get from diet

A

Essential Amino acids

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13
Q

is both essential because babies need to eat it and is also non-essential

A

Arginine

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14
Q

have all essential amino acids in amounts as needed by the human body

A

complete dietary proteins

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15
Q

very good protein alternative for vegans because it has a complete protein substitute

A

soy

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16
Q

only eat beans = kulang ng ?

A

methionine and tryptophan

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17
Q

only eat rice and oats = kulang ng ?

A

lysine

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18
Q

only eat corn

A

lysine and tryptophan

19
Q

only eat peas = kulang ng ?

A

methionine

20
Q

almonds and walnuts = kulang ng?

A

lysine and tryptophan

21
Q

Dipeptides have how many AAs?

22
Q

Oligopeptides have how many AAs?

A

3 - 10 AAs (Tripeptide and T peptide)

23
Q

How many AAs are there in Polypeptides?

A

11-100 AAs

24
Q

In naming Glutamate, it becomes?

25
In naming Glutamine, it becomes?
Glutaminyl
26
In naming valine, it becomes
Valinyl
27
structure where peptide bonds attach the a-amino group of one to the a-carbonyl group of another
Primary Protein Structure
28
folding of short (3-30 AA residues) sequences of polypeptides into geometrically ordered units
Secondary Protein Structure
29
type of Secondary Protein Structure that is the most common (Keratin is made up of 100% of these), spiral in shape, side chains are oriented outwards, and is 3.6 Amino Acids per term
Alpha Helix/ Helices
30
This type of secondary structure forms a zigzag or pleated pattern, can be parallel or anti-parallel, and are found in antibodies (immunoglobulins)
Beta Sheets
31
Shape of Tertiary structures and what are they stabilized by?
- 3D structure of the protein - stablized by: 1. Hydrophobic clustering forces 2. Disulfide bridges (Cystine) 3. Hydrogen bonds 4. Ionic interactions / salt bridges 5. Van der waals forces
32
Molecular chaperones assist in what?
assist in protein folding but are NOT the determinants of the final structure
33
this structure has 2 or more polypeptide chains forming one macromolecule
Quaternary Structure
34
Hemoglobin is an example of a quaternary structure because it has how many polypeptide chains?
Hemoglobin has 4 polypeptide chains: alpha 1 and 2, beta 1 and 2
35
any protein that's composed of more than one polypeptide chain is called?
Multimeric protein
36
these type of proteins are called 'enzymes' because they are the biologic catalysts in the body; one example is Pepsin
Catalysic Proteins
37
These type of proteins defend organisms against external agents of disease
Proteins with Immune Functions
38
One example of Transport Proteins that transport ferric/ iron ions
Transferric
39
What is the function of Messenger Proteins?
they give instructions to parts of the body (not all hormones are proteins)
40
Examples of Structural proteins
keratin and collagen
41
examples of movement proteins
myosin and actin
42
examples of Nutrient Proteins and what food they're found in
Casein - milk Albumin - eggs
43
Examples of Storage Proteins
myoglobin, hemoglobin, and ferritin (iron storage)
44
these proteins influence transcription from DNA to RNA and can either prevent or activate transcription
Regulatory Proteins