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Measuring A Computational Prediction Method For Fast Video
Predicting Many Properties of a Quantum System from Very Few MeasurementsProtein folding is the physical process by which a protein chain is translated to its native three-dimensional structuretypically 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. 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 ribosomethe 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 figureknown Methkd the native state.
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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[3] 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. Denaturation of proteins is a process of transition from the folded to the unfolded state.
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It happens in cookingin burnsin proteinopathiesand in other contexts. The duration of the folding process varies dramatically depending on the protein of interest.
When studied outside the cellthe slowest folding proteins require many minutes or hours to fold primarily due to proline isomerizationand must pass through a number of intermediate states, like checkpoints, before the process is complete. Understanding and simulating the protein folding process has been an important challenge for computational biology since the late s. The primary structure of a proteinits linear amino-acid sequence, determines its native conformation. The amino acid composition is not as important as the sequence.
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This is not to say that nearly identical amino acid sequences always fold similarly. Formation of a secondary structure is the first step in the folding process that a protein takes to assume its native structure. Characteristic of secondary structure are the structures known as alpha helices and beta sheets that fold rapidly because they are stabilized by intramolecular hydrogen bondsas was first characterized by Linus Pauling.
Formation of intramolecular hydrogen bonds provides another important contribution to protein stability.
The hydrogen bonds are between the amide hydrogen and carbonyl oxygen of the peptide bond.]
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