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Biochemistry > Chapter 3 > Flashcards

Chapter 3 Flashcards

1
Q

Structural proteins

A
  • collagen, elastin, keratin, actin, and tubulin
  • have high repetitive secondary structures and form supersecondary structures
  • these are also known as motifs
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2
Q

motif

A
  • highly repetitive secondary structures
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3
Q

collagen

A
  • three alpha helices make up most of connective tissue

- strength and flexibility

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4
Q

elastin

A
  • important in the extracellular matrix of connective tissue

- stretch and recoil like a spring

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5
Q

keratins

A
  • intermediate filaments found in epithelial cells
  • contributes to mechanical integrity
  • make up nails and hair
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6
Q

actin

A
  • make up microfilaments and thin filaments and are most abundant protein in eukaryotic cells
  • contain positive and negative sides that travel unidirectionally
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7
Q

tubuilin

A
  • make up microtubules

- provide structure and aid in the seperation of chromosomes during mitosis

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8
Q

myosin

A
  • are motor proteins that allow motor function and also cellular transportation
  • work to shorten sacromere during a muscle contraction (think filament)
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9
Q

dyneins

A
  • contain two heads
  • involved in sliding movements of cilia and flagella
  • bring vesicles towards the negative end of microtubule
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10
Q

kynesis

A
  • contain two heads

- bring vesicles towards the positive end of microtubules

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11
Q

Cell Adhesion molecules

A
  • (CAMS)
  • found on surface of cells and help them bind to extracellular matrix of other cells
  • three major are cadherins, integrins, and selecting
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12
Q

Cadherins

A
  • glycoproteins and mediate calcium-dependent cell adhesion

- hold similar cells together (N- cadherin –> nerves )

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13
Q

Integrins

A
  • membrane spannins chains called alpha and beta and are important in binding and communicating
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14
Q

Selectins

A
  • bind to carbohydrates that project from other cell surfaces
  • weakest forms of cams
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15
Q

immunoglobulins

A
  • are also known as antibodies
  • produced by B-cells and eliminate threats in the body
  • are Y shaped and contain two heavy and two light chains
  • contain and antigen-binding region at the tips of the “Y”
  • when antibody bind to target they become <b> antigens <b></b></b>
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16
Q

Antigen outcomes

A
  • neutralize the antigen
  • mark pathogen for descruction by other white blood cells
  • aggulating (clumping together) into larger insoluble protein
17
Q

Sinatrial Node

A
  • SA node in the heart (Pace maker)
  • contain nonspecific voltage gated sodium/potassium channels
  • when the voltage drops another action potential is fired to bring voltage back up
18
Q

Ligand-Gated channels

A
  • most of the neuromuscular junctions are ligand-gated

- GABA binds to chloride channel to open it

19
Q

G- protein-coupled receptors (GPCRs)

A
  • integral proteins that are involved in signaling
  • Gs: stimulates adenylate cyclase and increase cAMP
  • Gi: inhibits adenylate cyclase (antagonist to Gs) decreases cAMP
  • Gq: activates phospholipase C; cleaves phospholipid from membrane to form PIP2 which is then cleaved to form IP3 and DAG
20
Q

IP3

A
  • formed from when phospholipase C is activated by Gq which cleaves phospholipid from membrane to form PIP3 to be further cleaved into DAG and IP3
  • opens calcium channels in the endoplasmic reticulum
21
Q

electrophoresis

A
  • move proteins based on their net charge and their molecular weight
  • negative compounds travel towards the anode (+)
  • positive will migrate towards the cathode (-)
22
Q

Migration Velocity

A
  • V = Ez/f
23
Q

Polyacrylamide Gel Electrophoresis

A
  • PAGE
  • used to analyze proteins in their native state
  • limited to varying mass-to-charge and mass-to-size ratios
24
Q

SDS-PAGE

A
  • sodium dodecyl sulfate denatures proteins to be able to seperate them based on mass alone
  • non covalent bonds are disrupted
25
Q

retention time

A
  • this is the amount of time spent in the stationary phase
26
Q

Edman Degradation

A
  • use cleaved sequences up to 50 to 70 amino acids

- selectively and sequentially removing N-terminal amino acids of proteins

27
Q

Bradford Assay

A
  • stained with coomassie brilliant blue die
  • when unprotinated it exists in brown/green color
  • when deprotinated by protein it will turn blue
  • standard curve is then created with bradford reagent and measuring adsorbance
  • unknown is then placed in the same conditions and concentrations are based on the standard curve

Biochemistry (5 decks)

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