Module 02 - Microbial Biochemistry and Metabolism Flashcards
what are some reasons why the study of microbial physiology is often done using biochemistry?
allows of researchers to understand the biological processes of microbes and organisms
Common elements found in organic molecules
most abundant elements in cells are hydrogen, carbon, oxygen, nitrogen, and sulfur (macronutrients)
micronutrients/trace elements of a cell
Na, K, Mg, Z, Fe, Ca, Mo, Cu, Co, Mn, V
four most abundant elements in living matter
carbon, nitrogen, oxygen, and hydrogen, they have low atomic numbers, can form strong bonds with other atoms
biomolecules
part of living matter, contain C (C is unique, has 4 valence electrons)
carbon skeleton
(chain) carbon atoms bind together in large numbers
- shapes: straight, branched or ring-shaped (cyclic)
- many lengths but usually long
isomers
molecules with same atomic makeup but different structural arrangments of atoms
- important for chemistry because strucutre of molecule is directly related to its function
structural isomers
compounds that have identical molecular formulas but differ in the bonding sequence of atoms
stereoisomers
isomers that differ in spatial arrangements of atoms
- unique type - enantiomer, have characteristic of chirality
chirality
nonsuperimposable mirror images of each other in structures, important characteristic in biologically important molecule
functional group in organic molecules
atoms put into groups based on their chemical composition and chemical reactions they perform
explain the formation of biological macromolecules by dehydration synthesis
Most macromolecules are made from single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers. In doing so, monomers release water molecules as byproducts.`
carbohydrates
primarily a combination of carbon and water, they have empirical formula (CH2O)n, n=number of repeated units
- molecules are “hydrated” carbon atom chains and water molecules attach to each carbon atom
- ex. glucose/sugar
examples of monosaccharides
aldose and ketose
examples of polysaccharides
starch, glycogen, and cellulose (fiber)
monosaccharides
they are building blocks (monomers), produce and store energy
- classified based on number of carbons in a molecule
polysaccharides
(not sweet) not soluble in water, key functions are energy storage or structural support
explain why molecules with extremely diverse chemical structures can still be classified as lipids
lipids with long chain hydrocarbons terminated with a carboxylic acid functional group
- lipid molecules can also contain oxygen, nitrogen, sulfur and phospholipids
triacylglycerides
is formed when 3 fatty acids are chemically linked to a glycerol molecule
- three fatty acid chains are bound to glycerol by dehydration synthesis
phospholipids
phosphate group, two fatty acid carbon chains may be both saturated, both unsaturated or one of each
describe how phospholipids are used to construct biological membranes
they are used to construct biological membranes by their hydrophilic heads (water loving) and fatty acid tails that are hydrophobic (water hating)
amino acid
organic molecule in which a H atom, a carboxyl group (-COOH), and an amino group (-NH2) are all bonded to the same carbon atom, a carbon
side chain
fourth group thats bonded to the carbon varies among different amino acids.
primary structure
the sequence of amino acids that make up the polypeptide chain
secondary structures
chain is long, hydrogen bonding may occur between amine and carbonyl functional group within the peptide backbone (excluding R side group) which results in the localizing folding of a polypeptide chain into helices and sheets
alpha helix structure
held by H-bonds between the oxygen atom in carbonyl group of one amino acid and the hydrogen atoms of the amino group that is just 4 amino acid units farther along the chain
beta-pleated sheet
pleats are formed by similar H-bonds between continuous sequences of carbonyl and amino groups that are further seperated on the backbone of the polypeptide chain
tertiary structures
3D shape of a single polypeptide chain. the teritary structure is determined by interactions between amino acid residues that are far apart in the chain
- interactions give rise to protein tertiary structure (ex. disulfide bridges)
quaternary structures
proteins are assemblies known as protein subunits. proteins function well only when all subunits are present and appropriately configured
- protein consisting of more than one amino acid chain
- ex. hemoglobin has 4 globular protein subunits
conjugated proteins
non protein portion, carbohydrate attached called a glycoprotein
- if a lipid is attached its called a lipoprotein