[Demelerlab] Fwd: FW: Dissertation Defense - Nepomuceno

[Borries Demeler]

For those of you who worked on the Fibronectin experiment and those of you
who are simply interested in Fibronectin...
-Borries

---------- Forwarded message ---------
From: Sugden, Kent D. <kent.sugden at mso.umt.edu>
Date: Mon, Aug 14, 2023 at 4:27 PM
Subject: FW: Dissertation Defense - Nepomuceno
To: Berryman, Orion <Orion.Berryman at mso.umt.edu>, Bowler, Bruce <
Bruce.Bowler at mso.umt.edu>, Briknarova, Klara <klara.briknarova at mso.umt.edu>,
Chu, Xi <xi.chu at mso.umt.edu>, Cracolice, Mark <mark.cracolice at mso.umt.edu>,
Decato, Daniel <daniel.decato at mso.umt.edu>, DeGrandpre, Michael D <
michael.degrandpre at mso.umt.edu>, Demeler, Borries <
borries.demeler at mso.umt.edu>, edwaali at gmail.com <edwaali at gmail.com>,
Engstrom, Royce <Royce.Engstrom at mso.umt.edu>, Grina, Tyler <
tyler.grina at umconnect.umt.edu>, Hu, Lu <lu.hu at mso.umt.edu>, John, Eric <
eric.john at umconnect.umt.edu>, Lodmell, Stephen <stephen.lodmell at mso.umt.edu>,
Martin, Brooke D. <brooke.martin at mso.umt.edu>, Monroe, Jeffrey <
Jeffrey.Monroe at mso.umt.edu>, Palmer, Chris P. <chris.palmer at mso.umt.edu>,
Priestley, Nigel <nigel.priestley at mso.umt.edu>, Reimann, Melissa <
melissa.reimann at mso.umt.edu>, Riel, Asia Marie <asiamarie.riel at mso.umt.edu>,
Ryter, Kendal <kendal.ryter at mso.umt.edu>, Colenso, Sarah <
Sarah.Colenso at mso.umt.edu>, Smith, Garon <garon.smith at mso.umt.edu>, Sugden,
Kent D. <kent.sugden at mso.umt.edu>, Thomas, Aaron <aaron.thomas at mso.umt.edu>,
Wang, Dong <dong.wang at mso.umt.edu>, Yokelson, Bob <Bob.Yokelson at mso.umt.edu>








*Dissertation Defense | Precy Nepomuceno*



Title:  *Molecular Studies of Human Fibronectin*



Location*: Chemistry 212*



*Wednesday, August 16 at 9:00 a.m.*





Abstract:  Fibronectin is an extracellular matrix glycoprotein that plays a
major role in cell adhesion, cell growth and tissue organization. FN is
comprised of three types of modular repeats – type I (FN1), type II (FN2),
type III (FN3) – and a non-homologous variable region (V region) that can
contain 0 to 120 amino acid residues depending on alternative splicing.
Fibronectin contains several fibronectin type 3 (FN3) domains, which all
have a β-sandwich structure composed of three-stranded (β-strands A, B and
E) and four-stranded (β-strands C, D, F and G) β-sheets. FN3 domains are
susceptible to mechanical unfolding, and it has been hypothesized that
their unfolding leads to exposure of cryptic binding sites during
fibrillogenesis. In this research, we investigated the structure and
stability of the 11th FN3 domain of human fibronectin (11FN3) in the
context of its neighboring FN3 domains using X-ray crystallography, nuclear
magnetic resonance (NMR) spectroscopy and denaturant titration experiments.
Our results show that amino acid residues and domains at the C-terminus
affect the structure and stability of 11FN3. In addition to the study of
11FN3, we will also be describing here briefly two ongoing projects aiming
to determine the structure of intact, soluble fibronectin and the
interdomain interactions necessary for fibril formation using cryo-electron
tomography and optical tweezers. A complete understanding of the structure
and conformation of full-length FN will provide a better molecular picture
of the cellular matrix essential for various cellular processes.
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