Biochemsitry Flashcards
What are monosaccharides?
Carbohydrates composed of single sugar units.
Examples include glucose, fructose, and galactose.
What is a disaccharide?
A carbohydrate composed of two monosaccharides bonded together.
The bond is called a glycosidic linkage.
What is a monomer?
The smallest repeating unit of a polymer.
Example: Monosaccharide (glucose).
What is a polymer?
A large molecule composed of repeating units of smaller molecules (monomers).
What are lipids composed of?
Composed of carbon (C) and hydrogen (H) in varying proportions.
What are the functions of lipids?
Insulate against heat loss and form a protective cushion around major organs. Also provide energy (the most per gram, but not primary source of energy-carbs are)
They are also a major component of cell membranes.
What are the enzymes that hydrolyze proteins?
Proteases, such as Pepsin in the stomach, break down proteins into amino acids.
What enzymes hydrolyze lipids?
Lipases, which are hydrophilic and found in bile, target primary ester linkages and emulsify fats.
Which enzymes hydrolyze carbohydrates?
Maltase and Amylase (mouth and pancreas) are specific enzymes that break down carbohydrates.
What does Maltase do?
Maltase (with H2O) breaks Maltose into 2 glucose
Example: Maltase and water hydrolizes into 2 glucose molecules.
What is Chymosin and where does it come from?
Chymosin comes from microbes and helps make cheese.
What is the role of Proteases in beer production?
Proteases come from microbes and prevent cloudiness in beer.
What does Citrate Synthase do?
Citrate Synthase comes from fungi and makes citric acid used for jams.
List the essential amino acids.
- Isoleucine
- Leucine
- Lysine
- Threonine
- Phenylalanine
- Methionine
- Valine
- Tryptophan
What governs metabolism?
Metabolism is governed by the 2 laws of thermodynamics.
What is the law of conservation of energy?
Matter can’t be made or destroyed. As energy is converted, some is always ‘lost’, commonly in the form of heat.
What are enzymes?
Enzymes are proteins that have globular shapes with pockets or indentations known as active sites.
What is the enzyme-substrate complex?
The substrate and active sites join together to form an enzyme-substrate complex.
What are competitive inhibitors?
Competitive inhibitors are molecules of similar shape to the substrate that interfere with enzyme function and thus the chemical reaction.(can stop or slow down enzymes ability)
What is the behavior of enzymes?
Enzymes are free to bind to other substrates when they have completed their activity, are specific to their substrate, and are usually named after the molecule they cause to react.
What suffix do most enzymes have?
Most enzymes normally end in ‘ase’.
What does maltase do?(and H2O)
Maltase is an enzyme that breaks down maltose into 2 glucose molecules.
What is denaturation in proteins?
The process where proteins lose their shape and function due to exposure to extreme heat, major pH changes, or heavy metals, which disrupt bonds.
Denaturation alters the protein’s native structure, affecting its biological activity. ALTERS STRUCTURE AND FUNCTION
What are the primary functions of proteins?
- Transport O2 and CO2 throughout the body
- Structural components (hair, nails, skin, tendons)
- Enzymes
- Antibodies
- Hormones (chemical messengers)
Proteins play crucial roles in various biological processes.
What is the structure of proteins?
Proteins are composed of amino acids linked by peptide bonds, forming a linear sequence.
This sequence determines the protein’s unique properties and functions.
Describe the primary structure of proteins.
The simplest structure, consisting of a linear sequence of amino acids joined together by peptide bonds.
It is the result of protein synthesis.
What characterizes the secondary structure of proteins?
Hydrogen bonding occurs between the carbonyl oxygen of one amino acid and the nitrogen of another, forming shapes like ALPHA helices or BETA pleated sheets.
These structures contribute to the overall stability of the protein.
What is the tertiary structure of a protein?
The 3D structure formed by bends and twists due to various ionic bonds, covalent bonds, and hydrogen bonds among different regions of the amino acid chain.
Molecular chaperones assist in the proper folding of proteins.
What is the quaternary structure of proteins?
The structure formed when multiple tertiary structures cluster together, resulting in fibrous proteins like collagen and keratin or globular proteins like hemoglobin.
Quaternary structures are essential for the function of many multi-subunit proteins.
True or False: Proteins can only have one structure.
False
Proteins can have multiple levels of structure: primary, secondary, tertiary, and quaternary.
Fill in the blank: The _______ structure of proteins involves hydrogen bonding that leads to alpha helices or beta pleated sheets.
[secondary structure]
This structure is crucial for the stability and function of many proteins.
What is the nature of Hydroxy functional group?
Polar and hydrophilic. Creates alcohol.
Where is the Aldehyde functional group located?
At the end of the molecule. It is soluble and polar.
Where is the Ketone functional group located?
In the middle of the molecule. It is soluble and polar.
What are the characteristics of the Sulfhydryl functional group?
Polar and hydrophilic.
Hypertonic means…..
(In animal cells). Greater concentration (water) outside membrane- cells shrinks/sheivels - CRENATION
Hypotonic means…
(In animal cells) more concentration inside the cell, Less concentration (water) outside membrane - cells bloat up - LYSIS
Isotonic means…
Both solutions on both sides of membranes are equal. Concentrations equal, balanced. Cells remain normal
What is membrane-assisted transport? And what does it require?
Membrane-assisted transport is a process where a cell forms vesicles to surround incoming or outgoing material. It requires energy input.
What are the two main types of membrane-assisted transport?
- Moving materials into the cell: ENDOCYTOSIS.
- Moving materials out of the cell: EXOCYTOSIS -waste/large molecules leave cell by way of vesicles.
Used in animal cells for secreting hormones
Used in plant cells for the creating materials for constructing cell wall
Phagocytosis is…..
A form of endocytosis. The cell engulfs or “eats” something (debris, molecule, organisms.)
(ex. macrophages ingesting bacteria cells.)
Phagocytosis vs penocytosis
Both form of endocytosis
Penocytosis “drinks” and engulfs liquid and small particles in the liquid, phagocytosis “eats” and engulfs larger particles/organisms.
How do peroxisomes protect themselves from the reactive hydrogen peroxide they produce?
The enzyme catalase breaks down hydrogen peroxide within the peroxisomes.
Which organelle is involved in both the synthesis of bial acids and redox reactions that break down toxic substances?
Peroxisome
Lysosomes are like the cells _________. They…..
Recycling centre. They break down things like waste products and lipids
The central vacuole in plant cells……
stores water, nutrients, and waste products, and helps maintain turgor pressure, which supports the cell’s structure.
What organelle is involved in both the synthesis of bile acids, and redox reactions that breakdown toxic substances?
Peroxisomes
Compare the functions of 2 of the protien fibres in the cytoskeleton?
Microfilaments - cell shape and muscle contraction, assist in cell division
Intermediate filaments - maintain cell shape (scaffolding nucleus) and anchor some organelles
Use an example to describe the structure and function of cilia.
In respiratory tract, hair like structures on epithelial cells which help trap and move debris within mucus to be released (spit/cough).
Use an example to describe the structure and function of flagella.
Sperm cell, has a single tail like structure which helps it move. (flagellum -singular)
What cellular compensation makes up the inner shaft of cilia?
Microtubules - (type of protien fibre in cytoskeleton)
Just state the 3 types of endocytosis
Phagocytosis
Pinocytosis
RME(receptor mediated endocytosis)
