Amino acid sequence correlation in optimally designed proteins

dc.contributor.advisor	Franzese, Giancarlo
dc.contributor.author	Àguila Rojas, Joan
dc.date.accessioned	2019-09-13T13:52:39Z
dc.date.available	2019-09-13T13:52:39Z
dc.date.issued	2019-01
dc.description	Treballs Finals de Grau de Física, Facultat de Física, Universitat de Barcelona, Curs: 2019, Tutor: Giancarlo Franzese	ca
dc.description.abstract	Water plays a fundamental role in protein’s stability. Polymers with a segregation of hydrophilic amino acids in their surface have shown to have a larger stability region over changes in Pressure and Temperature in an aqueous solvent. This work expands the two-dimensional computational study made by Bianco, Franzese, Dellago and Coluzza to three dimensions, obtaining results consistent with their findings	ca
dc.format.extent	5 p.
dc.format.mimetype	application/pdf
dc.identifier.uri	https://hdl.handle.net/2445/139928
dc.language.iso	eng	ca
dc.rights	cc-by-nc-nd (c) Àguila, 2019
dc.rights.accessRights	info:eu-repo/semantics/openAccess	ca
dc.rights.uri	http://creativecommons.org/licenses/by-nc-nd/3.0/es/	*
dc.source	Treballs Finals de Grau (TFG) - Física
dc.subject.classification	Seqüència d'aminoàcids	cat
dc.subject.classification	Proteïnes	cat
dc.subject.classification	Treballs de fi de grau	cat
dc.subject.other	Amino acid sequence	eng
dc.subject.other	Proteins	eng
dc.subject.other	Bachelor's theses	eng
dc.title	Amino acid sequence correlation in optimally designed proteins	eng
dc.type	info:eu-repo/semantics/bachelorThesis	ca

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