protein folding is the process by which a sequence of amino acids - a protein - assumes a 3d structure, made up of "local" units of structures, often turns, sheets (beta sheets) and cylinders (alpha helixes) further arranged into a larger super structure. this is what confers functionality (binding, enzymatic reactions, etc) and dynamics (movements integral to the protein's functionality). the chemical principles that drive this are things like hydrophobic amino acids burying themselves away from a typical aqueous (water-based, or at least highly polar) environment, ionic pairings, hydrogen bonding (strong but not permanent bonds), etc.
in terms of predicting the protein's structure, the challenge is the sheer number of computations, the dynamics the protein goes through, and the effects of any environmental factors as the protein is synthesized or folded.
i spent much of a decade (mid 90's to early 00s) studying folding with an aim to getting into enzyme engineering. fun stuff, but i have since left biochem.
in terms of predicting the protein's structure, the challenge is the sheer number of computations, the dynamics the protein goes through, and the effects of any environmental factors as the protein is synthesized or folded.
i spent much of a decade (mid 90's to early 00s) studying folding with an aim to getting into enzyme engineering. fun stuff, but i have since left biochem.