Midterm Exam 1 Flashcards

1
Q

What are the 3 main tenets of cell theory?

A
  1. All living things are made from cells
  2. Cells are the smallest forms of life
  3. Cells form from existing cells through division
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2
Q

Scientific Method Steps

A
  1. Identify problem/gap in knowledge
  2. Develop hypothesis
  3. Experimentation
  4. Data analysis
  5. Reject or support hypothesis
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3
Q

Primary Protein Structure

A

Linear amino acid sequence

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4
Q

Secondary Protein Structure

A

Either spiral (alpha-helix) or sheet (beta-pileated sheet)

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5
Q

Tertiary Protein Structure

A

3D folding

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6
Q

Quaternary

A

Two or more polypeptide chains bind together

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7
Q

Dideoxy DNA Sequencing

A

Uses ddNTPs to pause transcription at each nucleotide, allowing for a list of target nucleotides

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8
Q

3 Approaches to identify a drug altering protein function

A
  1. Drug may inhibit homologous proteins to target one
  2. Use computer model to determine potential binding sites
  3. “Grocery store approach”
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9
Q

Light vs. electron microscopy

A

Light microscopy observes from 500nm to 5mm

Electron microscopy observes from 1nm to 100microm

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10
Q

Western Blotting

A

A large group of proteins is separated by electric current through gel, wells are probed with antibodies which will darken on nylon sheet when contacting the target well

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11
Q

What does the sgRNA in CRISPR Cas technology bind to?

A

The Cas9 protein and the target gene

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12
Q

Resolution

A

The ability to discern two nearby objects as being distinct

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13
Q

Contrast

A

How different one structure looks from another

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14
Q

Flagella microtubules vs. motor proteins

A

Microtubules are fixed in place, whereas the motor proteins are free to move along them

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15
Q

What is needed to move a lipid from one membrane leaflet to the other?

A

ATP and Flippase

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16
Q

Two main purposes of catabolic reactions

A
  1. Recycling organic monomers
  2. Synthesis of energy intermediates (ATP)
17
Q

3 types of membrane proteins

A

Transmembrane
Lipid-Anchored
Peripheral membrane

18
Q

ATP hydrolysis ____s with an endergonic reaction

A

Couples

19
Q

Enzyme-catalyzed reactions steps

A
  1. Protein binds to substrate
  2. Induced fit occurs
  3. Products form
  4. Products are released
20
Q

How do enzymes decrease energy of activation (Ea) for reactions?

A

Strain bonds, move reactants closer together, and change local environment (pH)

21
Q

Do enzymes effect direction of reactions

A

NO!

22
Q

How does sucrose enter a cell?

A

First, ATP is hydrolyzed as an H+ pump moves ions out of cell against the gradient via primary active transport.

Next, an H+/sucrose symporter moves both H+ ions and sucrose into the cell down the gradient through secondary active transport.

23
Q

Proteins are sorted to their correct destination through

A

Remaining in the cytosol, co-translational sorting (ER), or post-translational sorting (nucleus, peroxisome, mitochondria)

24
Q

Vesicular transport model vs. cisternal maturation model

A

Vesicles bud from ER, go to cis-med-trans Golgi (Golgi stays intact).

Vesicles from the ER fuse to form new cis Golgi, moving med to trans, losing trans compartment.

25
Q

Fluid Mosaic Model

A

Lipids, proteins, and carbohydrates can move freely in the membrane relative to each other

26
Q

Transport Proteins

A

Conformationally changes to switch access of solute from one side of membrane to the other (uniporter, symporter, antiporter)

27
Q

Competitive vs. Noncompetitive enzyme inhibition

A

Competitive inhibition binds to the active site of the substrate, effectively disabling the enzyme, increasing Km value.

Noncompetitive inhibition binds to the allosteric site, limiting function and decreasing Vmax value.

28
Q

Some enzymes require ____

A

Prosthetic groups (permanently attached), cofactors (temporarily attached), and coenzymes (organic molecule participating in the reaction but unchanged)

29
Q

Cells make ATP by

A
  1. Substrate-level phosphorylation, where enzyme transfers phosphate from organic molecule to ADP
  2. Chemiosmosis, energy of electrochemical gradient used to make ATP
30
Q

Regulation of metabolic pathways

A

Occurs through gene regulation, cell regulation, and biochemical regulation

31
Q

Proteasomes

A

Large complexes that break down misfolded proteins tagged with ubiquitin, and using protease enzyme, cleaves into amino acid to be recycled

32
Q

Autophagy

A

A worn-out organelle is enclosed by a membrane tubule which fuses to a lysosome and recycles the basic organelle components

33
Q

Pulse-Chase Assay

A

Radioactive amino acid injection quickly followed by a non-tagged amino acid injection. Samples of pancreatic cells taken periodically, stained, and observed under a transmission electron microscope (TEM)

34
Q

Passive Transport

A

Moving of molecules down a gradient, either with a channel protein (facilitated diffusion) or without (simple diffusion)

35
Q

Endocytosis

A

Moves material into cell via receptor-mediated processes, pinocytosis (cytosol liquids), and phagocytosis (large molecules like bacteria)

36
Q

Ribozymes

A

RNA catalysts used in important cell reactions (Altman’s discovery)