3.1-3.2 Flashcards
unique feature of each amino acid
R group
side chain
two common types of covalent bonds in proteins
peptide bonds
disulphide bonds b/w Cys
convention of writing proteins
amino terminal always written first
residue
individual aa when it is in a peptide
proteolysis
aka proteolytic cleavage
hydrolysis of a protein by another protein
specific means of cleaving peptide bonds
proteolytic enzyme
protease
protein that does the cutting
enzyme which cuts a protein
proteolytic cleavage
specific means of cleving peptide bonds
many enzymes cleave peptide bond adjacent to a specific aa
formation of peptide bond
lone pair on the amino group of 1 aa attacks the carboxyl group of the other aa
forming a N C C N C C pattern
trypsin cleavage
carboxyl side of Arg and Lys
chymotrypsin
cleaves adjacent to hydrophobic residues such as Phe
Cys special characteristics
has a reactive thiol ( SH) in its side chain
thiol aka sulfhydryl
reacts with thiol of another Cys to produce covalent S-S bond knwn as a disulphide bond
role of diS bond
important role in stabilizing tertiary protein structure
Cystine vs Cysteine
Cystine
refers to the molecule which is formed once the Cys residues are diS bonded to each other
Cysteine
refers to the individual aa
protein structure and function
each protein folds into a unique 3D structure that is required for protein to be functional
denatured
improperly folded proteins
are non functional