Određivanje glikoproteina iz humane plazme

master's thesis

• Title (english): Determining human plasma glycoproteins
• Author: Borna Rapčan
• Mentor: Gordan Lauc (mentor)
• Committee member: Gordan Lauc (predsjednik povjerenstva)
• Committee member: Lidija Bach-Rojecky (član povjerenstva)
• Committee member: Nada Vrkić (član povjerenstva)
• Granter: University of Zagreb; Faculty of Pharmacy and Biochemistry; (Department of biochemistry and molecular biology); Zagreb
• Defense date and country: 2019-07-08, Croatia
• Scientific / art field, discipline and subdiscipline: BIOMEDICINE AND HEALTHCARE; Pharmacy; Medical Biochemistry

Abstract

Glikozilacija je skup čestih i složenih kotranslacijskih/postranslacijskih kovalentih
modifikacija lipida i proteina. One su od velike važnosti jer utječu na funkciju i strukturu takvih
kompleksnih molekula. Istraživanja kompleksnih molekula su vrlo zahtjevna i često koriste
kombinacije metoda. Jedna od važnih grupa metoda koje se koriste u takvim istraživanjima su
bioinformatičke metode. One se uglavnom fokusiraju na analizu podataka i simulacije. Kako raste
broj radova na tu temu, raste i količina podataka koje bioinformatički alati trebaju koristiti te je
nužno razvijati nove alate koji će omogućiti lakše i brže istraživanje složenih mo lekula.
Ovaj diplomski rad je pokušaj razvijanja takvog alata koji olakšava pretraživanje
glikoproteoma UniProt baze podataka. Razvijeni alat je testiran na 592 anotirana glikoproteina
humane plazme. Računalnom analizom tih glikoproteina utvrđeno je da su oni većinom manji od
1000 aminokiselina i mase obično ispod 100 kDa. Također je utvrđeno da su njihove proteinske
strukture hidrofilne i da je najčešći tip glikozilacije zabilježenih proteina humane plazme Nglikozilacija.
Analiza je provedena i na peptidima proteina nastalih računalnom tripsinskom
razgradnjom proteina. Tom analizom je utvrđeno da je većina takvih peptida neglikozilirana,
većinom manje mase od 10 kDa, odnosno duljine 100 aminokiselina te da su manje hidrofilni od
izvornih glikoproteina od kojih potječu.

Abstract (english)

Glycosylation is a collection of complex cotranslational/posttranslational covalent
modifications of lipids and proteins. These modifications are of great importance as they affect the
function and structure of such complex molecules. Researching complex molecules is very
demanding and often requires combination of different types of methods. One such group includes
bioinformatic methods whose main goals are data analysis and simulations. As the number of
research papers grows, the amount of data on these molecules grows as well which consequently
requires better and faster tools for data analysis.
This Master’s thesis was an attempt of developing such a tool to improve the ones already
available for UniProt database. The developed tool was tested on a set of 592 annotated human
plasma glycoproteins. Computer analysis of the aforementioned set yielded the insight that most of
these proteins were smaller than 1000 amino acids with masses under 100 kDa. It has also showed
that most of these glycoprotein structures are hydrophilic in nature and that by far the most
common type of glycosylation is the N-glycosylation. Analysis of peptides acquried by computer
trypsine digestion was conducted as well. It showed that most of such peptides are much smaller
than their glycoprotein counterparts, mostly ranging in size under 10 kDa or 100 amino acids in
length and are less hydrophilic than full glycoproteomic structures.

• Keywords: glikozilacija; glikomika; humana plazma; bioinformatika
• Keywords (english): glycosylation; glycomics; human plasma; bioinformatics
• Language: croatian
• URN:NBN: urn:nbn:hr:163:524163
• Study programme: Title: Medical biochemistry; Study programme type: university; Study level: integrated undergraduate and graduate; Academic / professional title: magistar/magistra medicinske biokemije (magistar/magistra medicinske biokemije)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Open access
• Created on: 2019-09-26 13:43:00