Μεταπτυχιακές εργασίες ειδίκευσης
Τρέχουσα Εγγραφή: 30 από 800
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Κωδικός Πόρου |
000456149 |
Τίτλος |
Studying the effect of protein structure characteristics on the evolutionary rate of proteins |
Άλλος τίτλος |
Μελέτη της επίδραση χαρακτηριστικών δομής των πρωτεϊνών στον ρυθμό εξέλιξής τους |
Συγγραφέας
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Κυπριανίδη, Θεοδώρα Α.
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Σύμβουλος διατριβής
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Παυλίδης, Παύλος
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Μέλος κριτικής επιτροπής
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Παυλίδης, Ιωάννης
Ηλιόπουλος, Ιωάννης
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Περίληψη |
The aim of this study is to investigate if the evolutionary rate of proteins is affected,
firstly by structural characteristics of proteins and then by protein localization. Information about the evolutionary rate of proteins can provide valuable insights into
the functional and structural importance of specific protein regions; furthermore
it yields information about the evolutionary history, relationships and functional
divergence and finally it can be useful in evolutionary biology, bio-informatics and
drug discovery fields. Regarding structural characteristics of proteins, secondary
structure characteristics were studied, particularly Alpha helices and Beta sheets
in a data set that was extracted from the Protein Data Bank. The intention was
to investigate how the quantity of protein secondary structural elements affects its
evolutionary rate. We found that proteins containing more amino acids assigned
as Beta sheets rather than Alpha helices, tend to evolve faster. We classified our
proteins in KEGG pathways, in order to conduct pathway analysis, and compared
the evolutionary rates of proteins containing bigger percentage of Alpha helices
and Beta sheets within each pathway. From the Uniprot database we extracted
the possible locations for each protein and examined their impact on evolutionary rate. Furthermore, we performed a Gene Ontology analysis on both Alpha
helix and Beta sheet proteins to identify their corresponding biological processes,
molecular functions, and cellular components. This analysis aimed to investigate
whether these two types of proteins participate in different gene ontology terms,
which could potentially explain the observed differences in their evolutionary rates.
We found that B proteins are found more in the extracellular region while A proteins inside the cell; this could possibly explain their difference in the evolutionary
rates. For the second part of the study concerning protein localization we used a
data set from the G.Gkouridis lab (IMBB-FORTH), there are three protein locations, i.e., heavy membranes, light membranes and solution to investigate (i) if the
protein localization affects the evolutionary rate of proteins, and (ii) if secondary
structure elements in different locations affect the evolutionary rate.
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Φυσική περιγραφή |
70 σ. : πίν., σχήμ., εικ. ; 30 εκ. |
Γλώσσα |
Αγγλικά |
Θέμα |
A-helices |
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B-sheets |
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Evolutionary rate of proteins |
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Membrane proteins |
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Soluble proteins |
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Α-έλικες |
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Β-πτυχές |
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Διαλύτες πρωτεΐνες |
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Μεμβρανικές πρωτεΐνες |
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Ρυθμός εξέλιξης πρωτεϊνών |
Ημερομηνία έκδοσης |
2023-07-28 |
Συλλογή
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Σχολή/Τμήμα--Σχολή Θετικών και Τεχνολογικών Επιστημών--Τμήμα Βιολογίας--Μεταπτυχιακές εργασίες ειδίκευσης
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Τύπος Εργασίας--Μεταπτυχιακές εργασίες ειδίκευσης
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Μόνιμη Σύνδεση |
https://elocus.lib.uoc.gr//dlib/9/d/e/metadata-dlib-1686213384-351934-3375.tkl
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Εμφανίσεις |
478 |