Globular proteins fold into a native, biologically active, three-dimensional structure uniquely determined by amino acid sequence. The process of cotranslational folding takes place "in vivo" while the protein is being synthesized in the ribosome. In recent years cotranslational folding has become an object of study, also experimental. In this thesis work, it is proposed to adapt to the cotranslational framework a simple spin model in d=1, which was already used in the past to study the folding kinetics of proteins via Monte Carlo simulations.
Le proteine globulari ripiegano in una struttura tridimensionale nativa, biologicamente attiva, univocamente determinata dalla sequenza di aminoacidi. In anni recenti, è diventato oggetto di studio anche sperimentale il processo di ripiegamento cotraslazionale, che ha luogo "in vivo" mentre la proteina viene sintetizzata nel ribosoma. In questo lavoro di tesi, si propone di adattare al caso cotraslazionale un semplice modello di spin in d=1, già utilizzato in passato per studiare la cinetica di ripiegamento di proteine per mezzo di simulazioni Monte Carlo.
Modelli semplificati per il ripiegamento cotraslazionale di proteine
FELTRIN, ANTONIO
2021/2022
Abstract
Globular proteins fold into a native, biologically active, three-dimensional structure uniquely determined by amino acid sequence. The process of cotranslational folding takes place "in vivo" while the protein is being synthesized in the ribosome. In recent years cotranslational folding has become an object of study, also experimental. In this thesis work, it is proposed to adapt to the cotranslational framework a simple spin model in d=1, which was already used in the past to study the folding kinetics of proteins via Monte Carlo simulations.File | Dimensione | Formato | |
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https://hdl.handle.net/20.500.12608/41587