The illusive search for the lowest free energy state of globular proteins and RNAs.
As a consequence of the one-dimensional storage and transfer of genetic information, DNA→RNA→protein, the process by which globular proteins and RNAs achieve their three-dimensional structure involves folding of a linear chain. The folding process itself could create massive activation barriers that prevent the attainment of many stable protein and RNA structures. We consider several kinds of energy barriers inherent in folding that might serve as kinetic constraints to achieving the lowest energy state. Alternative approaches to forming 3D structure, where a substantial number of weak interactions would be created prior to the formation of all the peptide (or phosphodiester) bonds, might not be subjected to such high barriers. This could lead to unique 3D conformational states, potentially more stable than "native" proteins and RNAs, with new functionalities.
Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States. Electronic address: karpel@umbc.edu.
Richard L
RL
Karpel
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D017510:Protein Folding; D059370:RNA Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry
D018832:Molecular Chaperones; D012259:Ribonuclease, Pancreatic
3D structure; Folding; Proteins; RNA