2.2.9 proteins 2: protein structure & bonding Flashcards
primary structure
sequence of amino acids found in molecule
secondary structure
- coiling/folding of amino acid chain (often due to h bond formation between different parts of chain)
- main form: alpha helix or beta pleated sheet
tertiary structure
- overall 3-dimensional shape of a protein molecule
- due to interactions eg. h bonding, disulphide bridges, ionic bonds & hydrophobic interactions
quaternary structure
protein structure where protein consists of 1+ polypeptide chain
what does the order of amino acids in the primary structure determine
shape of protein molecule (through 2nd, 3rd, 4th structure)
what’s the alpha helix held by in the secondary structure (& between what)
- hydrogen bonds
- between -NH group of 1 amino acid & -CO group of another 4 places ahead in chain
what holds the beta pleated sheet together
- hydrogen bonds
- between the -NH group of 1 amino acid & -CO group of another further down strand
how are the alpha helix/beta pleated sheet made stable structures at optimal temp. & pH
due to the amount of hydrogen bonds formed
how is the precise shape of the tertiary structure held together
bonds between amino acids (which lie close to each other)
what may the tertiary structure adopt
- supercoiled shape (fibrous proteins)
OR - spherical shape (globular proteins)
what bond primarily holds the secondary structure
hydrogen bonds
what do hydrogen bonds form between
hydrogen atoms with slight positive charge & other atoms with slight negative charge
in amino acids, where do the h bonds form
form in hydroxyl, carboxyl & amino groups
- where can ionic bonds form?
- what do these ionise into?
- between carboxyl & amino groups that are part of R groups
- ionise into NH3+ & COO- = strongly attracted to each other
what does the R group of the amino acids cysteine contain
sulfur