proteins Flashcards
(biological molecules)
what is the monomer of a polypeptide chain?
amino acids
what are some examples of proteins in the body
hormones, haemoglobin, antibodies, enzymes, structural components
what do all amino acids contain?
a central carbon atom, an amine group (NH2), a carboxylic acid group (COOH) and an R group which varies between types
via what reaction do amino acids join?
condensation reaction
draw a dipeptide and label the peptide bond
…
what is the most simple amino acid and draw it
glycine, R group is just H
what is the primary structure of protein?
the order and number of amino acids in the polypeptide chain
what is the secondary structure of protein?
the shape that the polypeptide chain folds or coils into, either an alpha coil or a beta pleated sheet. these are stabilised by hydrogen bonds between oxygen and hydrogen
what is the tertiary structure of protein?
the folding of the polypeptide chain into a 3d shape. this is when the secondary structure allows the R groups to be close enough to interact
what are the four types of tertiary interactions in protein?
1- disulphide bonds in cystine
2- hydrogen bonds in R group
3- hydrophillic/hydrophobic
4- ionic bonds (electrostatically)
what is the structure of a globular protein?
compact, spherical, and water soluble. Formed when proteins fold into their tertiary structure (when R groups are close enough to interact). This is specifically due to the hydrophobic/hydrophilic interactions. The hydrophobic R groups on the amino acids avoid aqueous environments whilst the hydrophilic R groups stay outside of the protein. Therefore the proteins are soluble in water.
name three types of globular proteins
haemoglobin, insulin, catalase
what is a conjugated protein?
any globular protein that contains a non-protein component. e.g. lipoproteins have a lipid component
name three examples of fibrous proteins?
keratin, collagen, elastin
what is the structure of fibrous proteins?
formed from insoluble long molecules. Contain a high proportion of amino acids with hydrophobic R groups (don’t like water). The variety of amino acids is limited, and the polypeptide chain is often quite repetitive leading to very organised structures. Normally produce long, unfolded and strong proteins.