Important Terms and Definitions

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x Covalent bonds are strong bonds; are in nonpolar molecules
x An example of nonpolar molecules: Molecules that are made up of C and H are called
x Noncolvalent bonds are interactions between molecules or different parts of a large
biomolecule; weaker bonds
x An example of a polar molecule is water; partially positive H will interact with partially negative
O in a different water molecule (hydrogen bond)
x du}ÇZP]vv}v}ou}oµolv}Áv^]}o_
Common linkages between functional groups
x Ester: Alcohol +Carboxylic Acid
x Amide/Peptide: Carboxylic Acid +Amine
x Glucose is a 6-membered ring
x Oligosaccharides is a small chain of sugars; oligo = a few
x Glycogen is a polymer of glucose with alpha-1,6 and alpha-1,4 glycosidic linkages (alpha means
both atoms are located on the same(cis) side
x Starch, another polymer of glucose has only alpha-1,4 linkages
x Cellulose has beta-1,4 linkages
x Chitin, a polymer of N-acetylglucosamine also had beta-1,4 linkages
x Fats are normally saturated (i.e. no double bonds)
x Phospholipids have a hydrophilic polar head made up of a phosphatidyl choline and a
hydrophobic non-polar tail made up of 2 fatty acid chains; also contain a glycerol backbone
x There are two types of nucleotides: DNA (deoxyribonucleic acid) and RNA (ribonucleic acid);
DNA contains the 5-carbon sugar called deoxyribose, while DNA contains ribose as the 5-carbon
x Proteins are made up of amino acids as their monomers; there are 20 different types in which
only the R groups are different; amino acids are made up of an alpha carbon, a carboxyl group,
an amino group and a side chain
x In protein folding: Ribonuclease is an enzyme that chews up RNA
x Interactions between neighbouring residues leads to the initial events in folding to the
secondary structure of the protein
x Chaperones are proteins that aid/help in the folding of newly made proteins by preventing
inappropriate interactions
x Two types of common folding patterns into secondary structure: alpha-helix and beta-pleated
x The quaternary structure of proteins is the linking of multiple proteins to form large complexes
Á]Zuµo]o_µµv]_vmultiprotein complexes; includes intermolecular interactions of R
groups such as disulfide bonds and mostly noncovalent interactions
x Homodimer =2 of the same molecules attached together; haemoglobin is a heterotetramer t
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