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AGUILA ROJAS Joan.pdf (435.47 KB)

Document type

Bachelor thesis

Publication date

2019-01

Publication license

cc-by-nc-nd (c) Àguila, 2019
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/139928

Amino acid sequence correlation in optimally designed proteins

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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

Description

Treballs Finals de Grau de Física, Facultat de Física, Universitat de Barcelona, Curs: 2019, Tutor: Giancarlo Franzese

Subject

Seqüència d'aminoàcids, Proteïnes, Treballs de fi de grau

Subject (English)

Amino acid sequence, Proteins, Bachelor's theses

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Treballs Finals de Grau (TFG) - Física

Citation

ÀGUILA ROJAS, Joan. Amino acid sequence correlation in optimally designed proteins. [consulted: 12 of August of 2026]. Available at: https://hdl.handle.net/2445/139928

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