Chapter 2 Flashcards
4 types of non covalent bonds
-ionic
-hydrophobic
-hydrophilic
-van der Waals interaction
ionic bonds
electrons transferred to one nucleus rather than being shared
hydrophilic bonds
ions and polar molecules are readily soluble in water
hydrophobic bonds
non polar molecules which cannot interact with water, only associate with other hydrophobic molecules and result from absence of ionic and hydrogen bonds
van der Waals interaction
2 atoms close together, fluctuating electrical charges that are induced by proximity, very weak
what is an amino acid made of
carbon atom, carboxyl group, amino group, hydrogen atom, and distinctive side chain
different side chain categories
non polar, polar, basic, acidic
non polar side chain
-10 amino acids
don’t interact with water
hydrophobic
polar side chain
-5 amino acids
can form hydrogen bonds
hydrophilic
basic side chain
-3 amino acids
provides OH- ions in water and is hydrophilic
acidic
-2 amino acids
provides H+ ions in water and negatively charges also hydrophilic
4 different types of structures of protein
primary, secondary, tertiary, quaternary
primary structure
sequence of amino acids in its polypeptide chain
secondary structure
regular arrangement of amino acids with localized regions of polypeptide. there are 2 types
a helix - region of polypeptide chain coils around itself, the CO group of one peptide bond forming hydrogen bond
B sheet - formed when 2 of a polypeptide chain lie side by side with hydrogen bonds between them. Can be formed between several polypeptide strands, could be parallel or antiparallel
tertiary structure
describes overall folding of a single polypeptide chain as a result of interactions between side chains. The basic units are called domains (3_D structures). usually a combo of a helix and b sheets. The hydrophobic amino acids are in the inside while hydrophilic is on outside. The inside will have the a and b (secondary structures). On the outside it has polar and ionic bonds so that also determines the structure
