Sections I-IV Vocab Flashcards
hydrogen bonds
a hydrogen atom covalently bound to one electronegative atom also attracted to another electronegative atom
Electronegativity
elements that differ in their affinity for electrons. Share electrons unequally
Hydrophilic
form weak bonds to water molecules
Synthesis
A reaction that increases the structural complexity. An example is polymerization.
Polymerization
A large subset of group reactions
Condensation-Dehydration
Two molecules combine and small molecules are lost
Hydrolysis
Breakdown of an organic molecule by adding water H2O.
Polysaccharides
100 to 1000 monosaccharides linked together
Triglyceride
Three fatty acids linked to a glycerol molecule. Energy storage (fat),
Phospholipid
Principal component of cell membranes. Two fatty acids and a polar head group.
Peptide bond
amino groups joined together. the alpha amino group of one amino acid and alpha carboxyl group of a second.
Primary structure
Sequence of amino acids in its polypeptide chain
Secondary structure
Regular arrangement of amino acids. Localized regions of polypeptide: alpha helix and beta sheets
Alpha helix
region of polypeptide chain coils itself, with the CO group of one peptide forming an h-bond with NH
Beta sheets
two parts of a polypeptide chain lie side by side with hydrogen bonds between them
Tertiary structure
Folding of a single polypeptide. Interaction of the side chains of amino acids that live in different regions of the primary sequence. Structures are called domains. Localization of hydrophobic AA’s in the interior of the protein and the hydrophilic amino acids on the surface
Quaternary structure
Interactions between polypeptide chains in proteins composed of more than one polypeptide
Oxidation
loss of electron density, loss of oxygen or hydrogen
Reduction
gain of electron density, happens usually by gaining a hydrogen
Free energy
changes in enthalpy and entropy. Predicts whether or not the rxn is energetically favorable.
Activation energy
The energy required to reach the transition state. Role of an enzyme is to lower the activation energy by having multiple reactants come together.
Allosteric modification
“other site”. enzyme activity is controlled by binding small molecules to regulatory sites on the enzyme. Consists of multiple subunits and worlds directly on the affected protein and is faster.
Covalent modification
Needs to make the object before, turns it on and phosphorylates it. Longer lasting and less prone to fluctuation
Peripheral (Extrinsic) Membrane
Proteins that dissociate from the membrane following treatments with polar reagents, such as pH or high salt concentrations. Soluble in aqueous solutions.