Multimeric Protein structure that stabilizes primarily by non covalent interaction
Destruction of all the intermolecular forces except the Peptide bond.
Fundamental, functional and 3-D structural has characteristics of small, compact, globular protein
Accumulation of Amyloid plaques in brains as twisted b-pleated sheet fibrils with 3-D structure virtually identical to silk fibrils
Protein structure that stabilizes primarily by Hydrogen bonds
Responsible for the correct folding of proteins
It composed of 4 amino acids and plays a role in reversing the direction of polypeptides
Protein structure that contains disulfide bond as the only covalent stabilizing force
Interactions between opposite charged amino acids
Polar and uncharged , rigid and planar, trans configuration
Hydrogen bond between the Carbonyl oxygen and the α nitrogen of the 4th distant amino acid
R groups alternating above and below the chain may be parallel or antiparallel.
Protein structure that determines its folding and thus its function
Denaturation
Primary Structure
Domain
Quaternary Structure
Alpha helix
Tertiary Structure
Secondary Structure
Beta Bends
Alzheimer
Ionic bonds or SALT bridges
Chaperones
Beta Sheets
Peptide Bond
