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questions :protein folding
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[Member (365WT)]answers [Chinese ]Time :2019-10-31
Structure-determining function, knowing only the genomic sequence does not allow us to fully understand the function of the protein, and it is impossible to know how it works. Protein can assemble itself by the interaction in the cellular environment (specific pH, temperature, etc.) The process of self-assembly is called protein folding. The problem of protein folding is listed as an important topic of "biophysics in the 21st century". It is a major biological problem that has not been solved by the law of molecular biology. Predicting proteins from primary sequences The tertiary structure of molecules and further predicting their function is a challenging task.Studying protein folding, especially in the early stages of folding, that is, the folding process of the new peptide segment is a fundamental problem that finally clarifies the central rule. In this field, new discoveries in recent years have been able to spontaneously fold the new peptide segment. The concept has been fundamentally revised. Among them, X-ray crystal diffraction and various spectral techniques as well as electron microscopy have played an extremely important role. At the 13th International Congress of Biophysics, Nobel Prize winner Ernst emphasized in the report. It is pointed out that one of the main advantages of NMR for studying proteins is that it can study the dynamics of protein molecules in great detail, that is, the relationship between dynamic structure or structure motion and protein molecular function..Current NMR techniques have been able to observe the movement of protein structures in the time-second to picosecond time domain, including the movement of the backbone and side chains, and the folding and unfolding of proteins at various temperatures and pressures. Structural analysis of protein macromolecules is not just about solving a specific structure, but more about the fluctuations and movements of the structure. For example, enzymes and proteins that transport small molecules usually have two conformations, combined with the Unbound ligand.A structural fluctuation in a conformation is a necessary prelude to a conformational transformation. Therefore, it is necessary to combine spectroscopy, spectroscopy and X-ray structural analysis to study the balance of structural fluctuations, various intermediate states formed during conformational changes and changes. For example, in order to understand how proteins are folded, it is necessary to know the time scales and mechanisms of several basic processes during folding, including the formation of secondary structures (helix and fold), crimping, long-range interactions, and unfolded peptides. Complete collapse. A variety of techniques are used to study secondary processes such as fast NMR, fast spectroscopy (fluorescence, far ultraviolet and near-UV circular dichroism)...
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