PART 3 Flashcards

(41 cards)

1
Q

CLASSIFICATION (SHAPE)

▪️Keratin, Elastin (structural)

A

Fibrous

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2
Q

CLASSIFICATION (COMPOSITION)

▪️amino acids with additional components (nonproteins)
▪️Ex. Glycoproteins, phosphoproteins
▪️Lipoproteins
▪️Nucleoproteins

A

Conjugated

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3
Q

CLASSIFICATION (COMPOSITION)

▪️conjugated substances that is tightly bound to the protein (frequently found in enzymes)

A

Prosthetic Groups

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4
Q

CLASSIFICATION (COMPOSITION)

▪️an originally longer protein that was made shorter due to hydrolysis

A

Derived

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5
Q

CLASSIFICATION (SHAPE)

▪️Hemoglobin, Myoglobin, IG’S (Metabolic)

A

Globular

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5
Q

▪️Myoglobin
▪️Albumins, casein, most plant seed proteins
▪️Ferritin

A

Storage

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5
Q

▪️immunoglobulins and interferons
▪️prothrombin,fibrinogen, snake venom

A

Defence

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6
Q

▪️ Amino acid neurotransmitters
▪️Peptide Hormones - insulin, Glucagon

A

Messenger/ regulatory

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7
Q

▪️Collagen and Elastin,wool, silk, etc.
▪️Actin and myosin - added function for contraction - Ca2 dependent

A

Structural/ Contractile

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8
Q

WHAT FUNCTION

▪️Hemoglobin
▪️Transferrin

A

Transport

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9
Q

What are the 2 peptide hormones

A

Insulin
Glucagon

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9
Q

▪️Enzymes- help convert substrate into products

A

Catalytic

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10
Q

CLASSIFICATION (COMPOSITION)

▪️amino acids only
▪️Ex. Storage Proteins (albumins,globulins, gluten).

A

Simple

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11
Q

storage form of Fe2

A

Ferritin

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11
Q

WHAT FUNCTION

▪️Ferritin
▪️Ovalbumin
▪️Casein

A

Storage

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12
Q

▪️Hemoglobin
▪️Membrane channels and pumps

A

Transport

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13
Q

Transport form of Fe2

13
Q

WHAT FUNCTION

▪️Amylase
▪️Lipase
▪️Protease

14
Q

WHAT FUNCTION

▪️Actin
▪️Myosin

A

Contractile and Motor

15
Q

WHAT FUNCTION

▪️Insulin
▪️Glucagon
▪️T3 & T4

A

Hormonal/ Regulatory

16
Q

WHAT FUNCTION

▪️Immunoglobulins
▪️Antibodies
▪️Fibrinogen
▪️Thrombin
▪️Snake venom

17
Q

WHAT FUNCTION

▪️Nicotinic

18
Q

WHAT FUNCTION

▪️Collagen
▪️Elastin
▪️Keratin
▪️Fibroin

19
Q

Reagent that specifically cleaves at the C-terminal side of METHIONINE RESIDUES.

A

Cyanogen Bromide

20
Enzyme that cleaves peptide bonds at the C-terminal side of AROMATIC AMINO ACID like tryptophan, phenylalanine, and tyrosine.
Chrymotrypsin
21
Separation Methods
By polarity By charge By size
22
Types of Terminal Amino Acids ▪️include Edman reagent,sanger reagent, aminopeptidase
N-terminal
23
speed up chemical rxns but are not consumed in the process
Biologic Catalysts
24
all enzymes are proteins EXCEPT
Ribozymes (RNA molecules)
25
Enzyme that cleaves peptide bonds at the C-terminal side of BASIC AMINO ACID such as lysine and arginine.
Trypsin
25
Types of Terminal Amino Acids ▪️carboxypeptidase
C-terminal
25
▪️a molecule that enters an enzymatic reaction ▪️a molecule acted upon by the enzyme
Substrate
26
Nonproteins required by for enzymatic activity, can be organic or inorganic
Co-factors
27
Organic compounds from vitamins
Coenzymes/ Cosubstrates
28
This coenzyme, derived from niacin (Vitamin B3), is important in electron transfer/redox reactions.
NAD+ / NADH
29
This flavin-containing coenzyme, derived from riboflavin (Vitamin B2), is essential for redox reactions.
FAD / FADH2
29
This coenzyme is derived from pantothenate (Vitamin B5) and is involved in acetyl group transfer.
Coenzyme A (CoA)
30
This coenzyme has a source called S-adenosylmethionine (SAM) and is important in one-carbon metabolism.
Tetrahydrofolate (THF) (via SAM as methyl donor)
31
This coenzyme, derived from folic acid (Vitamin B9), is involved in methyl group transfer
Tetrahydrofolate (THF)
32
This coenzyme, derived from pyridoxine (Vitamin B6), is essential for amino group transfer.
Pyridoxal phosphate (PLP)
33
This coenzyme, derived from thiamine (Vitamin B1), is responsible for aldehyde transfer.
Thiamine pyrophosphate (TPP)