Molecular dynamics and free energy calculations in unconventional surfactants and proteins

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dc.contributor.advisor Giacometti, Achille it_IT
dc.contributor.author Carrer, Manuel <1993> it_IT
dc.date.accessioned 2019-02-17 it_IT
dc.date.accessioned 2019-06-11T08:42:03Z
dc.date.issued 2019-03-04 it_IT
dc.identifier.uri http://hdl.handle.net/10579/14398
dc.description.abstract Protein solvation is a fundamental process in biology and a detailed understanding of its basic principle is of paramount importance in current research. The study of the solvation properties of proteins in solvents different from water could lead to a better understanding of protein folding and the effects of non-bonded interactions in biological systems. Building upon past experimental and computational studies, the solvation free energies of the side chain analogues of 18 of the natural occurring amino acids are calculated using molecular dynamics simulations in cyclohexane and ethanol. Moreover the entropy-enthalpy balance is carefully assessed by singling out the energetic terms. In parallel, the aggregation properties of unconventional surfactants, synthesized here at the department of molecular science and nano-systems, are also studied. These molecules were experimentally shown to aggregate in an apolar medium without the presence of water. We implement molecular dynamics simulations also for this case both in water and in cyclohexane, and compute the critical micelle concentration (CMC) to guide new experimental studies in this framework. it_IT
dc.language.iso en it_IT
dc.publisher Università Ca' Foscari Venezia it_IT
dc.rights © Manuel Carrer, 2019 it_IT
dc.title Molecular dynamics and free energy calculations in unconventional surfactants and proteins it_IT
dc.title.alternative Molecular dynamics and free energy calculations in proteins and unconventional surfactants it_IT
dc.type Bachelor Thesis it_IT
dc.degree.name Scienze e tecnologie dei bio e nanomateriali it_IT
dc.degree.level Laurea magistrale it_IT
dc.degree.grantor Dipartimento di Scienze Molecolari e Nanosistemi it_IT
dc.description.academicyear 2017/2018, sessione straordinaria it_IT
dc.rights.accessrights closedAccess it_IT
dc.thesis.matricno 841235 it_IT
dc.subject.miur ING-IND/22 SCIENZA E TECNOLOGIA DEI MATERIALI it_IT
dc.description.note Protein solvation is a fundamental process in biology and a detailed understanding of its basic principle is of paramount importance in current research. The study of the solvation properties of proteins in solvents different from water could lead to a better understanding of protein folding and the effects of non-bonded interactions in biological systems. Building upon past experimental and computational studies, the solvation free energies of the side chain analogues of 18 of the natural occurring amino acids are calculated using molecular dynamics simulations in cyclohexane and ethanol. Moreover the entropy-enthalpy balance is carefully assessed by singling out the energetic terms. In parallel, the aggregation properties of unconventional surfactants, synthesized here at the department of molecular science and nano-systems, are also studied. These molecules were experimentally shown to aggregate in an apolar medium without the presence of water. We implement molecular dynamics simulations also for this case both in water and in cyclohexane, and compute the critical micelle concentration (CMC) to guide new experimental studies in this framework. it_IT
dc.degree.discipline it_IT
dc.contributor.co-advisor it_IT
dc.date.embargoend 10000-01-01
dc.provenance.upload Manuel Carrer (841235@stud.unive.it), 2019-02-17 it_IT
dc.provenance.plagiarycheck Achille Giacometti (achille@unive.it), 2019-03-04 it_IT


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