Front | Back |
Which amino acids have ionizable side chains?
|
Arginine, Lysine, Tyrosine, Cysteine, Histidine, Glutamic acid, & Aspartic acid
|
Nonpolar, Nonaromatic Amino Acids
|
Glycine, alanine, valine, leucine, isoleucine, methionine, & proline
|
Aromatic Amino Acids
|
Tryptophan, tyrosine, phenylalanine
|
Polar Amino Acids
|
Serine, threonine, asparagine, glutamine, cysteine
|
Negatively Charged (Acidic) Amino Acids
|
Aspartate (aspartic acid) & glutamate (glutamic acid)
|
Positively Charged (Basic) Amino Acids
|
Lysine, Arginine, Histidine
|
Hydrophobic Amino Acids
|
Amino acids w/ long alkyl side chains, found on interior of proteins. Include alanine, isoleucine, leucine, valine, phenylalaline
|
Hydrophilic Amino Acids
|
Amino acids w/ charged side chains, found on the exterior of proteins. Include positively charged histidine, arginine, and lysine, as well as negatively charged glutamate & aspartate. The amides glutamine & asparagine are also hydrophilic.
|
Primary structure of a protein is determined by ____. The primary structure of a protein is stabilized by ____.
|
The linear sequence of amino acids in a peptide. Peptide bonds
|
Secondary structure of a protein is determined by ____. The secondary structure of a protein is stabilized by ____. The 2 types of secondary structures are ____ & ____.
|
The local structure of neighboring amino acids. Hydrogen bonds between amino groups & nonadjacent carboxyl groups. Alpha helices & Beta-pleated sheets
|
Tertiary structure of a protein is _____. Tertiary structure is stabilized by ____.
|
The three-dimensional shape of a single polypeptide chain. Hydrogen bonds, hydrophobic interactions, disulfide links, & acid-base interactions (salt bridges).
|
Quaternary structure of a protein is due to ____.Quaternary structure is stabilized by ____.
|
The interaction between subunits in a multi-subunit protein (ex: hemoglobin consists of 4 distinct subunits that come together). Hydrogen bonds, hydrophobic interactions, disulfide links, & acid-base interactions (salt bridges).
|
Hydrophobic Interactions
|
Push hydrophilic amino acids to the outside of a protein, & hydrophobic amino acids to the inside of a protein.
|
Conjugated Proteins
|
Proteins w/ covalently attached molecules called Prosthetic Groups, which can be metal ions, vitamins, lipids, carbohydrates, or nucleic acids
|
Disulfide Bond
|
Occurs when to cysteine molecules are oxidized & create a covalent bond to form cystine.
|