Chapter 1- Proteins Flashcards
Proteins
contain C, H, O, N atoms (CHON)
Amino acids
are the monomers of proteins.
Contain Amino, Carboxyl, R-group, and Hydrogen atom.
20 amino acids with different R-groups.
Polypeptides
made up of amino acids (forms proteins)
Proteome
all of the proteins in a single cell. Can vary from cell to cell
Polypeptides
polymers of amino acids joined by peptide bonds.
Dehydration in polypeptides
is what forms peptide bonds and polypeptides
Hydrolysis in polypepetides
break peptide bonds
N-terminus (amino terminus)
side of polypeptide that ends with amino group
C-terminus (carboxyl terminus)
side of polypeptide that ends with carboxyl group
Primary structure of protein
sequence of a peptide determined by DNA.
All proteins have primary structure
Secondary structure
contains a-helix and B-pleated sheet.
hydrogen bonding between polypeptide backbones (no R-groups)
Tertiary Structure
3-D folding structure due to side chain interactions.
hydrophobic or hydrophilic spaces depending on R-groups.
Disulfide bonds are created by covalent bonding between R-groups of 2 cysteine amino acids.
Usually not covalent except for when there is disulfide bond
Hydrophobic
water-hating/nonpolar
Hydrophilic
water-loving/polar
Disulfide bonds
very strong bonds that act to hold tertiary structure pf polypeptide.
Cysteine
contains Sulfur (S) which allows for disulfide bonding in 3 structure
Quaternary structure
large proteins containing multiple polypeptide chains.
Tetramer protein
Has four subunits: primary, secondary, tertiary, quaternary
ex: hemoglobin
Globular protein
spherical caused by tightly folded polypeptide chains.
Usually hydrophilic (water soluble)
ex: hemoglobin, myoglobin
Fibrous protein
elongated providing structure support. hydrophobic on the outside making the water non-soluble
Proteins classified based on structure and composition
Structure: fibrous, globular, intermediate
Composition: can be simple (amino acids) or conjugated ( amino acids + other component)
Protein denaturation
the loss of protein function and structure.
Can denature by:
high or low temperature, ph changes, salt concentrations,
radiation
Only primary structure remains unaffected.
Cooking an egg in high heat disrupts IMF in egg’s protein causing it to coagulate, this is an example of
protein denaturation
Genome
All the DNA in a cell
Cysteine
Amino acid that Contains sulfur (S)
form covalent bonding
Can create disulfide bonds that are very strong