Protein structure

Protein folding is the physical process by which a protein chain is translated to its native three-dimensional structure, typically a “folded“ conformation by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA to a linear chain of amino acids. At this stage the polypeptide lacks any stable (long-lasting) three-dimensional structure (the left hand side of the first figure). As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding of many proteins begins even during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure), known as the native state. The resulting three-dimensional structure is determined by the amino acid sequence or primary structure (Anfinsen’s dogma). The correct three-dimensional structure is essential to function, although some parts of functional proteins may remain unfolded, so that protein dynamics is important. Failure to fold into native structure generally produces inactive proteins, but in some instances misfolded proteins have modified or toxic functionality. Several neurodegenerative and other diseases are believed to result from the accumulation of amyloid fibrils formed by misfolded proteins, infectious varieties of which are known as prions. Many allergies are caused by incorrect folding of some proteins, because the immune system does not produce antibodies for certain protein structures. Denaturation of proteins is a process of transition from the folded to the unfolded state. It happens in cooking, in burns, in proteinopathies, and in other contexts. The duration of the folding process varies dramatically depending on the protein of interest. When studied outside the cell, the slowest folding proteins require many minutes or hours to fold primarily due to proline isomerization, and must pass through a number of intermediate states, like checkpoints, before the process is complete. On the other hand, very small single-domain proteins with lengths of up to a hundred amino acids typically fold in a single step. Time scales of milliseconds are the norm and the very fastest known protein folding reactions are complete within a few microseconds. Understanding and simulating the protein folding process has been an important challenge for computational biology since the late 1960s. #proteins #Polypeptides #aminoAcids #hydrophobic #hydrophylic #peptide #proteinFolding #NikolaysGeneticsLessons #protein #polypeptide #aminoAcid #disulfideBridges #covalentBounding #ionicBounding #hydrophobicInteraction #proteinStructure #proteinSequence #ImidazolRing #Histidine #polypeptideChain #oligopeptide #hydrolysesSynthesis #condensationReaction #globularProteins #fibrousProteins #Genetics