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Il collasso idrofobico è una fase del ripi … Il collasso idrofobico è una fase del ripiegamento (folding) delle proteine nella quale le porzioni idrofobiche della catena polipeptidica si ripiegano verso l'interno della proteina. Le proteine non ripiegate (denaturate) disciolte nel citoplasma richiedono la formazione di un guscio di solvatazione nel quale le molecole di acqua sono disposte in modo ordinato tutto intorno alla proteina. Se due porzioni idrofobiche si avvicinano diminuisce anche la superficie esposta e quindi una parte delle molecole di acqua vengono rilasciate. Ciò comporta ad un aumento del disordine nel solvente e quindi ad aumento di entropia. Dal punto di vista termodinamico l'aumento dell'entropia è una condizione favorevole per la formazione e il corretto ripiegamento delle proteine.Tutto il processo non è dovuto ad un'attrazione fra i gruppi non polari ma alle proprietà dell'acqua. Tutto il processo di ripiegamento, fino alla formazione della proteina nativa, è accompagnato dall'espulsione di molecole d'acqua dalla proteina stessa.di molecole d'acqua dalla proteina stessa.
, Der hydrophobe Kollaps ist eine Hypothese zur Faltung von Proteinstrukturen aufgrund des hydrophoben Effekts.
, Hydrophobic collapse is a proposed process … Hydrophobic collapse is a proposed process for the production of the 3-D conformation adopted by polypeptides and other molecules in polar solvents. The theory states that the nascent polypeptide forms initial secondary structure (ɑ-helices and β-strands) creating localized regions of predominantly hydrophobic residues. The polypeptide interacts with water, thus placing thermodynamic pressures on these regions which then aggregate or "collapse" into a tertiary conformation with a hydrophobic core. Incidentally, polar residues interact favourably with water, thus the solvent-facing surface of the peptide is usually composed of predominantly hydrophilic regions. Hydrophobic collapse may also reduce the affinity of conformationally flexible drugs to their protein targets by reducing the net hydrophobic contribution to binding by self association of different parts of the drug while in solution. Conversely rigid scaffolds (also called privileged structures) that resist hydrophobic collapse may enhance drug affinity. Partial hydrophobic collapse is an experimentally accepted model for the folding kinetics of many globular proteins, such as myoglobin, alpha-lactalbumin, barstar, and staphylococcal nuclease. However, because experimental evidence of early folding events is difficult to obtain, hydrophobic collapse is often studied in silico via molecular dynamics and Monte Carlo simulations of the folding process. Globular proteins that are thought to fold by hydrophobic collapse are particularly amenable to complementary computational and experimental study using phi value analysis.perimental study using phi value analysis.
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| rdfs:comment |
Il collasso idrofobico è una fase del ripi … Il collasso idrofobico è una fase del ripiegamento (folding) delle proteine nella quale le porzioni idrofobiche della catena polipeptidica si ripiegano verso l'interno della proteina. Le proteine non ripiegate (denaturate) disciolte nel citoplasma richiedono la formazione di un guscio di solvatazione nel quale le molecole di acqua sono disposte in modo ordinato tutto intorno alla proteina. Se due porzioni idrofobiche si avvicinano diminuisce anche la superficie esposta e quindi una parte delle molecole di acqua vengono rilasciate. Ciò comporta ad un aumento del disordine nel solvente e quindi ad aumento di entropia. Dal punto di vista termodinamico l'aumento dell'entropia è una condizione favorevole per la formazione e il corretto ripiegamento delle proteine.Tutto il processo non è dovuto e proteine.Tutto il processo non è dovuto
, Hydrophobic collapse is a proposed process … Hydrophobic collapse is a proposed process for the production of the 3-D conformation adopted by polypeptides and other molecules in polar solvents. The theory states that the nascent polypeptide forms initial secondary structure (ɑ-helices and β-strands) creating localized regions of predominantly hydrophobic residues. The polypeptide interacts with water, thus placing thermodynamic pressures on these regions which then aggregate or "collapse" into a tertiary conformation with a hydrophobic core. Incidentally, polar residues interact favourably with water, thus the solvent-facing surface of the peptide is usually composed of predominantly hydrophilic regions.osed of predominantly hydrophilic regions.
, Der hydrophobe Kollaps ist eine Hypothese zur Faltung von Proteinstrukturen aufgrund des hydrophoben Effekts.
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| rdfs:label |
Hydrophober Kollaps
, Hydrophobic collapse
, Collasso idrofobico
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