Bio Paper One Application Flashcards
(498 cards)
How does the structure of the phospholipid bilayer contribute to its role in controlling what enters and exits the cell?
The phospholipid bilayer has a hydrophilic head and hydrophobic tails. The hydrophobic core prevents water-soluble (polar) substances, like ions and glucose, from easily passing through. Only small, non-polar molecules, like oxygen and carbon dioxide, can diffuse directly through the bilayer. Larger or polar molecules require transport proteins to cross the membrane, contributing to selective permeability
Why is cholesterol important in maintaining membrane fluidity, and how would its absence affect cell membrane function?
Cholesterol fits between the fatty acid tails of the phospholipids, restricting excessive movement and maintaining membrane fluidity. It prevents the membrane from becoming too fluid at high temperatures and too rigid at low temperatures. Without cholesterol, the membrane would be less flexible, affecting membrane stability, protein function, and transport of molecules.
How would the absence of channel proteins in the cell membrane affect ion movement and cellular function?
Provides a pathway for larger molecules by binding to them and changing their shape , and provide pathways for molecules that do not dissolve in lipids that would have difficulty passing through the hydrophobic core
Why can’t large polar molecules, like glucose, simply diffuse across the phospholipid bilayer?
Large polar molecules like glucose are hydrophilic and cannot pass through the hydrophobic core of the phospholipid bilayer. The non-polar tails of the phospholipids repel these polar molecules. Therefore, glucose requires carrier proteins or facilitated diffusion to move across the membrane.
What would happen to the cell if its surface membrane became permeable to all substances?
If the membrane were permeable to all substances, it would lose its ability to selectively regulate what enters and exits the cell. Harmful substances could freely enter, while essential molecules could leak out. This would disrupt homeostasis, leading to cell damage or death due to uncontrolled fluxes of ions, water, and other molecules.
Describe the role of glycoproteins in the cell surface membrane and how they contribute to cellular communication.
Glycoproteins, which are proteins with attached carbohydrate chains, play a key role in cell recognition and communication. They act as receptors for signaling molecules (like hormones) and help in cell-cell recognition (e.g., in immune responses). They enable cells to communicate with each other and respond to external signals, maintaining proper function and coordination in tissues
What impact does the temperature have on membrane fluidity, and how do phospholipids and cholesterol adapt to maintain membrane stability?
At higher temperatures, the phospholipids become more fluid, which could make the membrane too permeable. Cholesterol helps reduce this fluidity by pulling phospholipid tails closer together. At lower temperatures, phospholipids become more rigid, and cholesterol helps prevent them from packing too tightly, maintaining membrane flexibility. This balance ensures the membrane remains functional under varying temperature conditions.
How do surface proteins in the fluid mosaic model contribute to cell communication?
Surface proteins (also known as peripheral proteins) are found on the outer or inner surface of the cell membrane. These proteins can act as receptors, binding to specific signaling molecules like hormones which triggers a response inside the cell. They are also involved in cell recognition, helping cells identify each other and communicate during immune responses or tissue formation.
Why is it important for the cell membrane to maintain selective permeability, and how do surface proteins aid in this function?
Allows needed ions substances and nutrients in the cell, whilst isolating harmful or unnecessary substances ,it controls what goes in and out the cell maintaining the right balance of nutrients ions and waste products in and out of the cell.
What is the basic structure of an amino acid, and why is this important for protein formation?
An amino acid has a central carbon atom (C) bonded to four groups: an amino group (NH₂), a carboxyl group (COOH), a hydrogen atom (H), and a variable R group (side chain). The R group differs between amino acids and determines their properties (e.g., hydrophobic, hydrophilic). Amino acids link together via peptide bonds to form polypeptides, which fold into specific shapes to form proteins. This structure is essential because the sequence and properties of amino acids determine the shape and function of the protein.
How do peptide bonds form between amino acids, and what type of reaction is involved?
Peptide bonds form between the carboxyl group of one amino acid and the amino group of another during a condensation reaction. In this reaction, a molecule of water (H₂O) is removed, and the amino acids are joined by a peptide bond, creating a growing polypeptide chain. The reverse reaction, hydrolysis, breaks peptide bonds during protein digestion.
Describe the primary structure of a protein and explain why it is important.
The primary structure of a protein is the sequence of amino acids in a polypeptide chain, determined by the DNA sequence of a gene. This sequence dictates how the polypeptide will fold into its secondary, tertiary, and quaternary structures, ultimately determining the protein’s 3D shape and function. Even a small change in the primary structure (like a mutation) can dramatically affect the protein’s function.
What is the secondary structure of a protein, and how are hydrogen bonds involved?
The secondary structure refers to the regular folding or coiling of the polypeptide chain into structures like alpha-helices or beta-pleated sheets, which are stabilized by hydrogen bonds between the backbone atoms of the polypeptide. These hydrogen bonds form between the C=O group of one amino acid and the N-H group of another, providing stability to the structure without involving side chains (R groups).
How does the tertiary structure of a protein differ from the secondary structure, and what interactions are responsible for it?
The tertiary structure is the overall 3D folding of a polypeptide chain, determined by interactions between the R groups (side chains) of the amino acids. These interactions include:
Hydrogen bonds between polar R groups.
Ionic bonds between oppositely charged R groups.
Disulfide bridges (covalent bonds) between cysteine residues.
Hydrophobic interactions between non-polar R groups.
This structure determines the protein’s specific shape and function, such as the active site of an enzyme.
What is the quaternary structure of a protein, and how does it relate to proteins like hemoglobin?
The quaternary structure involves the association of two or more polypeptide chains to form a functional protein. In hemoglobin, for example, four polypeptide subunits come together, each with an iron-containing heme group that binds oxygen. The quaternary structure allows for cooperative binding of oxygen, which is crucial for efficient oxygen transport in the blood.
Explain how you would test for the presence of proteins using the Biuret test, and describe what a positive result looks like.
The Biuret test is used to detect the presence of proteins. Here’s how you conduct it:
Add a small amount of the Biuret reagent (a mixture of sodium hydroxide and copper sulfate) to the sample.
If proteins are present, the copper ions in the reagent will form a complex with the peptide bonds, causing the solution to turn purple.
Positive result: The solution changes from blue to purple, indicating the presence of proteins (peptide bonds). Negative result: The solution remains blue, indicating no proteins are present.
How do disulfide bonds contribute to the stability of the tertiary structure of a protein?
They are strong covelant bonds they stabilise the structure by holding parts of the polypeptide chain together , they do not get effected by fluctuating ph or high temps ,so maintain stable structure in harsh conditions.
What role do proteins play as enzymes, and how does their structure relate to their function?
Proteins act as enzymes, which are biological catalysts that speed up chemical reactions in the cell. The tertiary structure of an enzyme determines the shape of its active site, which is specific to the substrate it binds to. The enzyme’s ability to fold into the correct shape is crucial for its function, as the shape of the active site must match the substrate in a lock-and-key or induced-fit model for the reaction to proceed efficiently.
What is the significance of denaturation in proteins, and how can factors like heat or pH lead to it?
Denaturation occurs when a protein loses its natural structure due to external factors like heat, pH changes, or chemicals. This can disrupt hydrogen bonds, ionic bonds, and hydrophobic interactions, causing the protein to unfold and lose its functional shape. For example, heating an enzyme can denature it, making it unable to bind its substrate, thus losing its catalytic activity. Denaturation is often irreversible.
Why are fibrous proteins like collagen suited for structural roles, and how does their structure differ from globular proteins?
Fibrous proteins such as collagen have long rope like structures that provide strength and support in tissue ,they are made up of long repetitive amino acids forming parallel fibres . Globular proteins are spherical and soluble in water ,they have hydrophilic amino acids on their surface but hydrophobic amino acids in centre
How does the structure of haemoglobin as a globular protein aid its function
Haemoglobin function is to bind to oxygen , the hydrophilic region allows it to be soluble in plasma for easy transport across circulatory system to transport oxygen to different areas in the body. The hydrophobic area of the structure helps stabilise its 3d structure ensuring it folds correctly maintaining its shape so that oxygen can bind to hydrophobic pockets so that haemoglobin can carry the oxygen without it needing to diffuse in the blood directly .
Proteins perform a wide range of functions in living organisms. Explain how the structure of a protein determines its function, using examples such as enzymes, transport proteins, and antibodies.
The structure of a protein is directly related to its function, as its specific 3D shape allows it to perform a particular task.
Enzymes: The shape of the active site, determined by the protein’s tertiary structure, allows enzymes to bind specific substrates and catalyze reactions. For example, amylase breaks down starch into sugars because its active site fits the starch molecules perfectly.
Transport Proteins: Carrier and channel proteins in the cell membrane have specific shapes that allow them to transport ions and molecules across the membrane. For example, the sodium-potassium pump actively transports sodium out of the cell and potassium into the cell, maintaining essential ion balances.
Antibodies: These proteins have a specific structure that allows them to bind to foreign antigens with high specificity. This binding is crucial for the immune response, as antibodies help neutralize pathogens or mark them for destruction by other immune cells.
What are the main structural components of a lipid?
Lipids consist of glycerol and fatty acids. Triglycerides, a common type of lipid, are made from one glycerol molecule bonded to three fatty acids.
Why are triglycerides efficient molecules for energy storage?
Have a high ratio of energy storing carbon-hydrogen bonds to carbon atoms so are excellent source of energy. They have a low mass to energy ratio making them good storage molecules as can store a lot of energy in smaller space (beneficial to animals who have reduced mass they have to carry around).triglycerides are large and non polar (hydrophobic) and insoluble in water does not affect water potential in cells.
Triglycerides have a high ratio of hydrogen to oxygen atoms so release water when oxidised (provide important water source beneficial for organisms in dry deserts)