Macromolecules/ Organic Chemistry Flashcards
(28 cards)
Organic chemistry
The chemistry of carbon compounds.
Study of carbon compounds
What are the sources of variation we identified in class for organic molecules?
Hydrocarbons: which contains only carbon and hydrogen.
Hydrophobic because the c-c and c-h bonds are nonpolar.
What are enantiomers?
Each of a pair of molecules that are mirror images of each other
What are functional group?
- have specific chemical and physical properties
- are the regions of organic molecules which are commonly reactive
- behavior consistently from one organic molecule to another.
Their number and arrangement determines the unique chemical properties of the molecules of which they occur.
Functional groups
Small characteristics groups of atoms that are frequently bonded to the carbon skeleton of organic molecules
What types of reaction build macromolecules?
Dehydration reaction build macromolecules.
Reaction that removed a molecules of water as two molecules become bonded together
What types of reaction break down macromolecules?
Hydrolysis is chemical breakdown of a compound due to reaction of water
How is the term polymer different from the term macromolecules.
Macromolecules are giant molecules formed by the joining of smaller molecules. ( dehydration reaction, proteins, carbohydrates or nucleic acid.)
Polymer a large consisting of many identical or similar monomers linked together by covalent bond.
What is a monomer?
The subunit that serves as a building block of a polymer.
Identify each category of macromolecules that we discuss in class.
Carbohydrates
Lipids
Proteins
Nucleic acids
Describe the structure and each, using specific examples and identifying building blocks of macromolecules
Carbohydrates- sugars and their polymers( build sugar)
Lipids- fats, mostly hydrophobic molecules mainly made of hydrocarbons.
Proteins- (polypeptides)small building blocks called amino acids.
Nucleic acids- (DNA, RNA, ATP) the sequence of amino acids is programmed by genes( polymers).
Describe the biological function of carbohydrates
Single monosaccharides- simple sugar.
Storage polysaccharides energy
Function of lipids
Energy stared cell membranes harmonies vitamin D. Non polymer built from similar monomers.
Proteins function
Enzymes structure gene regulation transport membrane hormone receptor, communication cellular. Motor movement.
Nucleic acids function
Stores information recipe of proteins Building proteins ATP is on energy molecules Polymers nucleic acids Monomers- nucleotide
Describe the structure of storage polysaccharides as compared to structural polysaccharides
Storage polysaccharides- angles of bonds make helical shape that can branch, starch( plant ) and Glycogen(animal).
Structural polysaccharides- bonds in chain that do not branch (can bond to structural polysaccharides next to them) cellulose in plant ( parallel stands) chitin used as exoskeleton in insects.
Describe the difference between saturated and unsaturated fats.
Saturated fat- no double fonds between carbon atoms in tail. With hydrogen.( solidify at room temperature, animal fats, atherosclerosis)
Unsaturated fat- chain of carbon contains double bonds. Not saturated with hydrogen. ( most will not solidify at room temperature, plant and fish oils.)
What is the most important feature of a protein?
The most important role is building enzymes chemical catalysts that speed regulate virtually all chemical reaction in the cells.
How does a proteins get its shape?
The way it folds and twists determines which molecules can bind to it.
Amino acids
Describe primary proteins structure
The sequence( order) of the amino acids can affect the secondary structure.
Secondary proteins structure
Hydrogen bonds from between areas along the amino acid chain at regular intervals forming spirals and folds
Shape alpha helix and pleated sheet.
Tertiary proteins structure
Irregular bending and folding from many types of bonding.
Overall folding of the molecules
Due to multiple of types of bonds.
Quaternary proteins structure
Polypeptide chains attached to each other.
Two tertiary polypeptide bond together to form quaternary.
What factors can influence a protein’s shape?
Factors affecting shape
- pH, salt concentration, temperatures
- denaturation