Amino Acid Structures + Structures

Arginine (Arg; R) -positive, hydrophilic

Histidine (His; H) - positive, hydrophilic

Lysine (Lys; K) - positive, hydrophilic

Aspartic Acid (Asp; D) - negative

Glutamic Acid (Glu; E) - negative

Serine (Ser; S) - polar

Threonine (Thr; T) - polar

Asparagine (Asn; N) - polar

Glutamine (Gln; Q) - polar

Tyrosine (Tyr; Y) - polar

Alanine (Ala; A) - nonpolar

Isoleucine (Ile; I) - nonpolar

Leucine (Leu; L) - nonpolar

Methionine (Met; M) - nonpolar

Phenylalanine (Phe; F) - nonpolar

Tryptophan (Trp; W) - nonpolar

Valine (Val; V) - nonpolar

Cysteine (Cys; C)

Glycine (Gly; G)

Proline (Pro; P)

Primary Structure

structure that determines linear sequence and has peptide bonds (N→ C terminus)

Secondary Structure

structure where protein begins to fold with hydrogen bonds (e.g. alpha helix + beta pleated sheet from polypeptide chains)

Tertiary Structure

3D structure of a protein with V.D.W., ionic, hydrogen bonds and disulfide bridges; interactions between R groups of same polypeptide chain

Quaternary Structure

structure made up of subunits of polypeptide chains formers dimers (2), trimers (3), tetramers (4)