Exam 2 Flashcards

(37 cards)

1
Q

What does the lipid bilayer consist of?

A

Phospholipids which have hydrophilic heads (water attracting) and hydrophobic tails (water repelling)

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2
Q

What is the Hydrophobic Core?

A

The hydrophobic tails form the inner part of the lipid bilayer, creating a hydrophobic core.

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3
Q

Channel Proteins Structure and Function

A

Forms pores or tunnels through the lipid bilayers, allowing certains ions and molecules to pass through the membrane and down their concentration or electrochemical gradient (passive transport). Highly selective channels, only allowing specific ions (such as sodium, potassium, or calcium) or small POLAR molecules (like water) to pass.

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4
Q

Channel Proteins

A

Forms pores or tunnels through the lipid bilayer, allowing certain ions or molecules to pass through the membrane and down their concentration or electrochemical gradient. Highly selective, allows only specific ions such as sodium, potassium, or calcium to pass.

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5
Q

Ion Channels

A

Channels open in response to a signal (voltage changes) permitting specific ions to flow in and out of the cell.

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6
Q

Aquaporins

A

Specialized channels for water molecules, allowing rapid movement of water across the membrane while excluding other solutes.
Mode of transport: Facilitated diffusion, no energy (ATP) is required

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7
Q

Carrier Proteins

A
  • Carrier proteins bind to the specific molecules or ions they are transporting.
  • They undergo conformational change that allows the molecule to be transported across the membrane.
  • Can move substances both passively and actively.
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8
Q

Passive Transporters: Carrier Protein

A

These carrier proteins move substances down their concentration gradient through facilitated diffusion, similar to channels but with a slower rate due to the conformational requirements. For example, glucose transporters (GLUT) facilitate the diffusion of glucose.

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9
Q

Active Transporters

A

These proteins actively pump molecules against their concentration gradient, requiring energy, usually from ATP hydrolysis. Examples include sodium-potassium (Na+/K+ pump), which actively moves sodium out of and potassium into the cell, maintaining the electrochemical gradient necessary for cellular functions.

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10
Q

Symporters

A

These transporters move two different molecules in the same direction across the membrane. For example, the sodium-glucose symporter uses the energy from sodium ions moving down their gradient to transport glucose into the cell against its concentration gradient

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11
Q

Antiporters

A

These transporters move two molecules in opposite directions. For example, the sodium-calcium exchanger moves sodium into the cell while transporting calcium out, helping regulate calcium levels.

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12
Q

Passive Transport

A

Refers to the movement of solutes across the membrane without the use of energy. It helps the cell maintain balance with its environment for essential substances like nutrients, gases, and waste products.

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13
Q

Simple Diffusion

A

Small, nonpolar molecules like oxygen (O₂), carbon dioxide (CO₂), and lipophilic (fat-soluble) molecules can move directly through the lipid bilayer, bypassing the need for transport proteins. No energy or transport proteins are required.

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14
Q

Facilitated Diffusion

A

Larger or polar molecules (such as glucose, amino acids, or ions) cannot diffuse through the lipid bilayer on their own. They require the assistance of transport proteins—either channel proteins or carrier proteins.

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15
Q

Active Transport

A

Active transport refers to the movement of solutes against their concentration gradient, from an area of low concentration to an area of high concentration, and requires the input of energy, typically in the form of ATP.

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16
Q

Sodium-potassium pump

A

Example of primary active transport. It pumps 3 sodium ions (Na) out of the cell and 2 potassium ions (K) into the cell, both against their concentration gradient.

17
Q

Concentration Gradient

A

The concentration gradient refers to the difference in the concentration of a solute between the inside and outside of the cell.

18
Q

Membrane Potential (Eletrical Gradient)

A

An electrochemical gradient is the combined effect of two gradients:
- Concentration gradient: The difference in the concentration of ions across a membrane.
- Electrical gradient: The difference in charge (voltage) across the membrane.
Together, these gradients drive the movement of ions, such as sodium (Na⁺) or potassium (K⁺), across the membrane, influencing processes like ATP production, nerve signaling, and muscle contraction.

19
Q

Electrochemical Gradient

A

The electrochemical gradient is the combination of the concentration gradient (chemical) and the membrane potential (electrical). It determines the net driving force for the movement of charged solutes (ions) across the membrane.

20
Q

Cystic Fibrosis

A

Genetic disorder that affects thee respiratory and digestive system due to the mutations in the CFTR gene. The CFTR protein is a channel that regulates the movement of chloride ions across ephithelial cell membrane. When it malfunctions, it leads to the production of thick, sticky mucus that causes various symptoms

21
Q

What are the general function of proteins?

A

Protein have many functions such as enzymatic activity, structural support, and transport.

22
Q

What is the function of proteins in enzymatic activity?

A

Proteins act as enzymes to catalyze biochemical reactions, speeding up metabolic processes. Examples include amylase (breaks down starch) and DNA polymerase (synthesizes DNA strands).

23
Q

What is the primary structure of a protein?

A

The primary structure is the linear sequence of amino acids in a protein, determined by the gene encoding it and stabilized by peptide (covalent) bonds.

24
Q

What is the role of proteins in structural support?

A

Proteins like collagen and actin provide structural support, with collagen strengthening connective tissues and actin forming the cytoskeleton, which maintains cell shape.

25
How do proteins function in transport?
Proteins facilitate the movement of molecules, with hemoglobin transporting oxygen in the blood and membrane proteins like the sodium-potassium pump maintaining ion gradients across cell membranes.
26
What is the secondary structure of a protein?
The secondary structure involves localized folding, such as α-helices and β-pleated sheets, stabilized by hydrogen bonds between the backbone atoms.
27
What is the tertiary structure of a protein?
The tertiary structure refers to the 3D shape of a single polypeptide chain, stabilized by hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges between R-groups.
28
What is the quaternary structure of a protein?
The quaternary structure is the arrangement of multiple polypeptide chains into a single functional complex, such as hemoglobin, stabilized by similar interactions found in tertiary structures.
29
How do noncovalent hydrogen bonds contribute to protein folding?
Hydrogen bonds stabilize protein folding by forming between backbone atoms in second.ary structures and between side chains in tertiary and quaternary structures.
30
How can changes in pH influence protein folding?
pH changes alter the ionization states of amino acid side chains, disrupting hydrogen bonds and destabilizing protein structure, potentially causing denaturation.
31
What happens when a mutation like A300Q occurs in the PAH gene?
The mutation changes alanine (nonpolar) to glutamine (polar), disrupting protein folding or stability, leading to reduced PAH function, which can cause PKU by accumulating phenylalanine.
32
What is PKU (Phenylketonuria)?
PKU is a genetic disorder caused by PAH gene mutations that lead to nonfunctional phenylalanine hydroxylase, causing phenylalanine buildup, which can harm the brain.
33
How do chaperone proteins assist with mutant CFTR proteins in cystic fibrosis?
Chaperones bind to the misfolded CFTR protein, attempting to refold it and prevent aggregation. If refolding fails, the protein is degraded, contributing to cystic fibrosis symptoms.
34
What is the Unfolded Protein Response (UPR)?
UPR is activated when misfolded proteins accumulate. It increases folding capacity, inhibits protein synthesis, and promotes degradation of faulty proteins. If unresolved, it can lead to apoptosis.
35
How does the proteasome degrade misfolded CFTR proteins?
The proteasome identifies misfolded CFTR proteins through ubiquitination, unfolds them, and degrades them into smaller peptides within its catalytic core.
36
What alternative mechanism do cells use for protein degradation besides the proteasome?
Cells use lysosomes via autophagy - Damaged proteins are enclosed in autophagosomes - Autophagosomes fuse with lysosomes - Lysosomes degrade bulk material using digestive enzymes
37