Protein Flashcards

(55 cards)

1
Q

comes from the greek word proteos, meaning “primary” or “first place”

A

Proteins

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2
Q

proteos meaning

A

primary or first place

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3
Q

For structural and functional purposes

A

proteins

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4
Q

Proteins are made up of building blocks called

A

amino acids

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5
Q

How many amino acids are linked together in different combinations

A

20 different amino acids

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6
Q

proteins found only in animals and they usually serve as structural entities. They are normally insoluble to water

A

Fibrous proteins

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7
Q

Usually do not serve a structural function, they act as transporters, and they are usually water-solluble

A

Globular proteins

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8
Q

2 general categories of proteins

A

Fibrous protein
Globular protein

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9
Q

Proteins in immune system

A

Antibodies - fight invaders
Compliment system - system of 20 protein molecules that are activated during infections

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10
Q

signaling proteins

A

cytokines - communicate with other cells

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11
Q

proteins in the blood

A

hemoglobin - transports oxygen
fibrinogen - clots blood
albumin - maintain proper amount of liquid in blood

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12
Q

Enzymes

A

Digestive enzymes - helps break down food

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13
Q

Acts as enzymes, act as receptors, form channels for substances to move through membrane, 3 types of proteins: peripheral, integral, lipid-bound protein

A

Cell membrane

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14
Q

Structural proteins

A

Cytoskeleton - network of protein filaments and tubules that maintain cell shape
Keratin - found in skin, hair, and nails
Collagen - provides strength
Elastin - provides flexibility

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15
Q

Proteins in the muscle

A

Actin and Myosin - interactions with each other for muscle movement
Myoglobin - release oxygen to muscles
Ferritin - stores and release oxygen

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16
Q

Biological catalysts - speed up chemical reactions

A

Enzymes

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17
Q

Digestive enzymes aid in hydrosis

A

Lipase
Amylase
Lactase
Protease

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18
Q

Molecular biology

A

Polymerase
Ligase

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19
Q

Industry

A

Dairy, baby food, rubber, beer, photography, contact lenses cleaner

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20
Q

Support
Structural proteins

A

Keratin - hair and nails
Collagen - supports ligaments, tendons, and skin
Silk - cocoons and spider webs

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21
Q

transport molecules in the blood

A

hemoglobin - transport oxygen in the blood

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22
Q

allow substances to enter and exit the cell

A

channeln and carrier proteins in the cell membrane

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23
Q

Defense
Combat bacteria and viruses

24
Q

Regulation
Intercellular messengers that influence metabolism

25
regulates the amount of glucose in the blood and in cells
Insulin
26
In presence of this determines the height if an individual
Human growth hormone
27
Built into the membranes of nerve cells
Receptor proteins
28
Detect chemical signals (neurotransmitters) release by other nerve cells
Receptor proteins
29
Motion Muscle contraction -make up muscle fibers
Actin and myosin
30
Allow cell components to move from place to place
Motor proteins within the cell
31
Move the cell
Flagella
32
move contents around the cell
cilia
33
Scientist determined thisb 20 set of amino acids and labeled these sets as
the magic 20
34
cross links between sulfurs in amino acids
disulfide bridges
35
linking NH2 ofnone amino acid to COOH of another
peptide bonds
36
2 types of protein synthesis
Transcription Translation
37
The synthesis of RNA from a DNA template where the code in the DNA is converted into a complementary RNA code
Transcription
38
The synthesis of a protein from an mRNA template where the code in the mRNA is converted into an amino acid sequence in a protein
Translation
39
Structures of protein
Primary Structure Secondary structure Tertiary Structure Quaternary strucure
40
This structure refers to its amino acid sequence. Amino acids in polypeptides and proteins are joined together by peptide bonds between the carboxyl and amino groups adjacent amino acids
Primary structure
41
folding along short sections of polypeptide
Local folding
42
this protein only have secondary structure
fibrous proteins
43
2 types of protein folding
alpha helix Beta-pleated sheet
44
refers to short range, periodic folding elements that are common in proteins.
Secondary Structure: a Helix
45
adopts a cylindrical spiral structure in which there are 3.6 aas per turn
a(alpha) helix
46
adopts an extended conformation. strands tend to occur in pairs or multiple copies that interact with one another via H-bonds perpendicular to the axis of each strand
B (beta) pleated sheets
47
Whole molecule folding Created when the 2ndary structure fold and form bonds to stabilize the structure into a unique shape anchored by disulfide bridges Van der Waals Force (velcro)
Tertiary Structure
48
Have tertiary structure
Globular (spherical) proteins
49
Refers to the folded 3d structure of a protein. It is also known as the native structure or active conformation.
Tertiary structure
50
Tertiary structure is aka
native structure or active conformation
51
2 or more tertiary folded peptide subunits bonded together to make a functional protein
Quaternary structure
52
hiw many polypeptide does a hemoglobin and collagen has
4 3
53
Multisubunit (multimetric) proteins have another level of structural organization known as
Quaternary structure
54
refers to the number of subunits, their relative positions, and contacts between the individual monomers in a multimetric protein.
Quaternary structure
55
Unfolding a protein/changes the shape
Denaturation of protein