The amino-acid sequence (or primary structure) of a protein
predisposes it towards its native conformation or conformations.
It will fold spontaneously during or after synthesis. While
these macromolecules may be regarded as "folding themselves",
the mechanism depends equally on the characteristics of the
cytosol, including the nature of the primary solvent (water or
lipid), macromolecular crowding, the concentration of salts, the
temperature, and molecular chaperones. Subscribe in a reader
Most folded proteins have a hydrophobic core in which side chain
packing stabilizes the folded state, and charged or polar side
chains on the solvent-exposed surface where they interact with
surrounding water molecules. It is generally accepted that
minimizing the number of hydrophobic side-chains exposed to
water is the principal driving force behind the folding process,
although a recent theory has been proposed which reassesses the
contributions made by hydrogen bonding The strengths of hydrogen
bonds in a protein vary,