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