PP4 Flashcards
What are the 4 macromolecules? What is a macromolecule?
proteins
nucleic acids
carbohydrates
lipids
Macromolecules are large organic polymers formed from monomers, or subunits. Formed by polymerization reactions, which are chemical reactions that link two or more small molecules to form larger molecules with repeating subunits
What breaks down macromolecules?
Catabolic pathways break down these macromolecules. We derive energy from the catabolism of glucose and we use the energy, available as ATP, to make our own macromolecules through anabolic (building) pathways.
What are the basic functions of each macromolecule?
- proteins: Provide structural support and act as catalysts that facilitate chemical reactions
- nucleic acids: Encode and transmit genetic information
- carbohydrates: Provide source of energy and make up the cell wall in bacteria, plants and algae
- lipids: Make up cell membranes, store energy, and act as signaling molecules
Most macronutrients are polymers. What is a polymer? How are the formed?
- complex molecules made up of repeated simpler unites (monomers) connected by covalent bonds.
Mono = one; poly = many; mer(e) = unit or part - Polymers are formed by a polymerization reaction by connecting monomers forming covalent bonds. In this step, water is removed, so the reaction is called a dehydration synthesis or condensation reaction.
How to you build and break polymers?
Building polymers: Dehydration (removing water) synthesis or Condensation reaction
Breaking down polymers: Hydrolysis reaction Hydro = water; lysis = cutting [hydrolysis adds water molecule, breaking bond]
What are the 8 proteins and an example of each?
- Enzymatic proteins: acceleration of chemical reaction (ex. enzyme)
- Defensive proteins: protect against deases (ex. antibodies)
- Storage proteins: storage of amino acids (ex. casein)
- Transport proteins: transports substances (ex. hemoglobin)
- Hormonal proteins: coordination of an organism activity (ex. insulin)
- Receptor protein: repose of cell chemical stimuli (ex. receptors)
- Contractile proteins: movement (ex. actin and myosin)
- Structural proteins: support (keratin)
What are the 4 components attached to the a carbon?
- animo group (a base)
- carboxyl group (acid)
- hydrogen
- R group (4 types) [One amino acid has hydrogen as an R group]
Where do the 20 animo acids used differ?
- only in their R group
R-groups can be:
- hydrophilic
- hydrophobic
- acidic
- basic
- “special”
What is a peptide bond? The formation of a peptide bond is what type of reaction?
A covalent bond that connect 2 animo acids together. Peptide bonds form between the carboxyl group of one amino acid and the amino group of the other.
Condensation reaction since it releases water and makes the 2 molecules “smaller”
What is a dipeptide and polypeptide bond?
dipeptide: molecule formed of two amino acids
polypeptide: molecule formed of many amino acids
Explain the primary structure of the protein.
- its a linear sequence connected by peptide bonds
- Each protein has a unique sequence of amino acids
- Each polypeptide chain has an N- terminal (amino) and a C-terminal (carboxyl).
Explain the secondary structure of the protein.
- Interactions between stretches of amino acids lead to the formation of α helix and β sheets.
- formation of H-bonds between the carbonyl group in one peptide bond and the amide group in another
Explain the tertiary structure of the protein. Hydrophobic? Hydrophilic?
- Three-dimensional confirmation of a single polypeptide chain, usually made of several secondary structure elements
- Determined by the spatial distribution of hydrophilic and hydrophobic “R groups” along the molecule
- Hydrophobic amino acids cause the polypeptide to fold
- Hydrophilic amino acids allow the formation of H-bonds (and other bonds) that hold cause the polypeptide together
(Ultimately determines the protein’s function!!)
Explain the quaternary structure of the protein. Dimeric and trimeric protein?
proteins that are composed of 2 or more polypeptide chains or subunits, each of which has a tertiary structure, and that also come together to form a higher-order quaternary structure
A dimeric protein has 2 N-terminals and 2 C-terminals.
trimeric protein has 3 C-terminals and 3 N-terminals) [antibodies]
What is denaturation? What is the primary structure preserved? What about renaturation?
- Secondary, tertiary and quaternary (if present), determine its function
- Most proteins can be unfolded, or denatured, by chemical treatment or high temperature that disrupt all but the peptide bonds. The primary structure is preserved, i.e., the amino acids remain connected.
- Denatured proteins lose their functional activity.
- Renaturation to a functional form rarely takes place.
What are the 2 types of nucleic acids?
DNA and RNA
- > they differ in function and structure
- > DNA (a polymer) consists of monomers called deoxyribonucleotides (dNTPs), which consist of a deoxyribose sugar, phosphate (1, 2, or 3) and a nitrogenous base
What is the difference between purines and pyrimidines?
Purines: have a double ring structure.
Pyrimidines: have a single ring structure.
What are the 4 things that DNA contains?
- all the information to program a cells activity
- directions for its own replication
- is copied and passed on from one generation to the next
- contains genes that code for instructions to make proteins
How are nucleotides linked together to form a DNA single strand?
phosphodiester bonds: is a covalent bond that connects the 3’ carbon of one nucleotide to the 5’ carbon of the next nucleotide in the line through the 5’ phosphate group. This creates the sugar-phosphate backbone of the DNA strand.
- Stable bonds that can withstand stress (heat and pH)
- Give a DNA strand polarity: Negative phosphate group found on the 5’ carbon, Hydroxyl group found on the 3’ carbon
Explain the structure of DNA.
- DNA in cells consist of two strands of nucleotides twisted around each other in the form of a double helix
- The two sugar-phosphate backbones run in opposite directions: antiparralel