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Cell Physiology > Chapter Five And Six > Flashcards

Chapter Five And Six Flashcards

1
Q

Amino acid sequence determines what

A

Protein shape

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2
Q

What type of boding maintains shape

A

Noncovalent bonding

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3
Q

What type of bonding determines flexibility and rotation

A

Covalent

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4
Q

What do you want the easiest shape to form

A

Least energy required to make

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5
Q

What are molecular chaperones

A

Help the protein fold correctly

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6
Q

What are some diseases that are caused by improper protein folding

A

Alzheimer’s, Huntington’s, creuzfeldt-Jakob

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7
Q

What are prions

A

Misfolding proteins in the brain

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8
Q

Symptoms of Parkinson’s

A

Resting tremor, rigidity, festinating Gate, dementia

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9
Q

Aggregates of misfolded proteins- prions- form what

A

Amyloid fibrils

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10
Q

What are some shapes of proteins

A

Globular, fibrous, sheets,rings, and spheres

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11
Q

What can help determine shape of protein in lab

A

X-ray crystallography, NMR, and threading

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12
Q

What are some folding patterns of proteins

A

Alpha helix, beta sheet and H bonding

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13
Q

Examples of alpha helix

A

Keratin

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14
Q

Where can keratin be found

A

Nails, hair, skin, horns

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15
Q

Example of beta sheet

A

Fibroid

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16
Q

Where can fibroin be found

A

Silk

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17
Q

Hydrogen bonds in alpha helixes bond with every what number of peptide bond

A

Fourth

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18
Q

What is a coiled coil

A

Two alpha helixes that tuck in the hydrophobic areas

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19
Q

In beta sheets, how do H bonds form

A

Between peptides that are laying side by side

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20
Q

Anti parallel has what size loop

A

Short loop

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21
Q

Parallel beta sheet has what type of loop

A

Long

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22
Q

What is an example of beta sheet

A

Antifreeze protein

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23
Q

What is a protein domain

A

Independently folding polypeptide chain from which other proteins are constructed

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24
Q

What are targets for proteins

A

Unstructured protein regions

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25
Q

What are unstructured protein regions

A

Larger proteins with numerous domains connect by polypeptide chain containing unstructured sequences

26
Q

Are unstructured protein regions tucked into the protein

A

No, not folded

27
Q

What are flexible tethers

A

Provide movement and flexibility, help scaffold proteins bring proteins together, intracellular signaling pathways, assist elastin in forming rubberlike fibers

28
Q

Unstructured regions in UPRs can do what

A

Bend, flex, wrap around larger target proteins

29
Q

What are protein families

A

Groups of proteins with similar amino acid sequences and conformations, look similar and have similar functions

30
Q

What are examples of protein families

A

Serine proteases, chemotrypsin, trypsin, elastase

31
Q

Dimer and tetrameres are examples of

A

Large protein molecules containing weak noncovalent forces

32
Q

Example of large protein molecule

A

Hemoglobin

33
Q

Filaments, sheets or spheres are larger proteins that depend on

A

Complimentary binding sites and have indefinite number of bindings

34
Q

Elongated fibrous proteins spans

A

Long distances

35
Q

Examples of elongated fibrous proteins

A

Keratin, extracellular matrix, collagen and elastin

36
Q

What are extracellular proteins

A

Covalent cross linkages that strengthen proteins by formation of disulfide bonds that are found extracellularly

37
Q

How do protein binding work

A

Proteins interact with ligands through weak or strong binding

38
Q

Proteins have what type of binding with noncovalent bonds

A

Complementary binding

39
Q

Function of antibodies

A

Hunt pathogens

40
Q

Describe binding of antibodies

A

Tight and specific

41
Q

Structure of antibody

A

Y shaped

42
Q

Where is the specificity of binding in antibodies

A

At the y ends

43
Q

How does binding occur in antibodies

A

Triggered by an immune response

44
Q

Enzymes as catalysts are highly…

A

Specific for a single reaction

45
Q

Function of lysozyme

A

Break down polysaccharide chains

46
Q

How do lysozymes break down polysaccharides

A

Add water to molecule

47
Q

Examples of non protein molecular coenzyme assistants

A

Retinal, heme molecules, and coenzymes

48
Q

Catalytic activities of enzymes are regulated by

A

Gene expression, compartmentalizations, feedback regulation

49
Q

What are the different types of binding in catalytic enzymes

A

Allosteric binding, phosphate binding

50
Q

What are allosteric enzymes

A

Enzymes with two binding sites

51
Q

How do allosteric enzymes work

A

Bind in both binding sites then change conformations

52
Q

Function of phosphorylation

A

Involves attachment of a phosphate group to an amino acid side chain

53
Q

Phosphorylation changes what in protein

A

Activity

54
Q

Kinases function

A

Add phosphate

55
Q

Phosphotases function

A

Take away phosphate

56
Q

How do GTP binding proteins work

A

GTP in protein becomes hydrolyzed to form GDP inactivating the protein then GDP leaves protein, GTP then reactivates protein

57
Q

Function of motor proteins

A

Cellular movement

58
Q

What are protein machines

A

Large complexes that allow proteins to act in a coordinated manner due to hydrolysis of GTP or ATP

59
Q

Example of covalent modifications in protein machines

A

Receptor tyrosine kinase

60
Q

How are proteins studied in vitro

A

Cultured cells, differentiated properties are maintained, raw materials

Cell Physiology (16 decks)

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