Protein Structure and Function Pt1 Flashcards
8 types of proteins
Structural proteins
Enzymes
Transport proteins
Storage proteins
Motor proteins
Receptor proteins
Signal proteins
Hehe regulatory proteins
What catalyses peptide bonds?
Ribosomes (ribozyme)
What are smaller polypeptides called?
Oligopeptides and peptides
AA sequence affects protein structure
Where does peptide bond formation take place?
At the carboxyl or amino group of the amino acid
What gives an amino acid its unique properties?
The R group does depending on the side chains such as acidic,basic, uncharged, or non polar
What is the pKa
It’s the acid dissociation constant that describes the acidity of a particular molecule
Dissociation of carboxyl and amino groups
(H+ given off or added)
What is the isoelectric point (pI)?
It’s the pH where the amino acid has no net electrical charge (where it is neutral)
Describe the backbone of the peptide
The peptide bond is rigid and planar and C-N bond inflexible
What’s bonds are involved in protein folding?
Covalent bonds such as disulphide bridge bond and many weak non covalent bonds such as ionic bonds, H bonds, VDW bonds.
Misfolded proteins can lead to diseases, what helps with protein folding?
Chaperone proteins help with folding