Protein Flashcards
9 essential amino acids
histadine isoleucine leucine lysine methionine valine phenylalanine threonine tryptophan
5 non-essential amino acids
alanine aspartic acid glutamic acid serine asparginine
6 conditionally essential amino acids
arginine cysteine glutamine glycine proline tyrosine
protein chains of AAs joined together called
peptides
what kind of reaction forms peptides
condensation reaction
what bonds join amino acids
peptide bonds
2 AAs joined by peptide bond called
dipeptide
aspartic acid bonded to phenylalanine forms a dipeptide known as
aspartame
3 AAs joined by peptide bond called
tripeptides
L-cysteine, L-glutamate & glycine form a tripeptide called
glutathione
can amino acids act as buffers
yes
what is denaturing
unfolding proteins by breaking the peptide bonds - makes them unable to function
ex of denaturing agents
heat organic solvents mechanical mixing strong acids or bases detergents heavy metals
ex of a denatured protein
cooked egg white
gene mutation causes protein misfolding causes
disease
eg - amyloid protein in alzheimers
Functions of proteins
structure of body tissues - collagen movement - actin & myosin fibres carrier molecules - haemoglobin storage molecules - ferritin fluid balance in blood - albumin enzymes hormones - insulin immune function - antibodies clotting mechanisms alternative energy source (carb more efficient) control of gene expression cell membrane receptors
building blocks of protein
amino acids
describe protein digestion
HCL in stomach converts pepsinogen > pepsin, protein chains broken down into polypeptides
small intestine cck & secretin released, stimulates pancreatic juices
trypsin & chymotrypsin continue chopping up polypeptides
peptidases in small intestine break down further
amino acids & small peptides absorbed into bood
