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Difference between revisions of "User:Natalie Bamford"

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[[File:NatalieBamford.png|200px|right]]
 
[[File:NatalieBamford.png|200px|right]]
  
'''Natalie Bamford''' did her undergraduate degree at the [http://biochemistry.utoronto.ca/ University of Toronto in Biochemistry]. She then completed her graduate work supervised by [[User: Lynne Howell|Lynne Howell]] conducting research out of the Hospital for Sick Children. This led to her obtaining her PhD in Biochemistry from the University of Toronto in 2019. Her research focused on the carbohydrate active enzymes involved in exopolysaccharide production used by microbes in biofilm formation. This included structural and biochemical characterization of glycoside hydrolases <cite>Bamford2015 Snarr2017 Little2018 LeMauff2019 Bamford2019</cite>, carbohydrate esterase <cite>Little2014 Little2014b Little2015 Bamford2020</cite>, and a carbohydrate binding module <cite>Bamford2020</cite>. Natalie's studies helped in the creation of three GH families ([[Glycoside Hydrolase Family 135|GH135]], [[Glycoside Hydrolase Family 153|GH153]], [http://www.cazy.org/GH166.html GH166]), one CE family (CE18) and one CBM family ([[Carbohydrate Binding Module Family 87|CBM87]]). She is now a postdoctoral fellow at the University of Dundee with [https://www.lifesci.dundee.ac.uk/people/nicola-stanley-wall Nicola Stanley-Wall].  
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'''Natalie Bamford''' did her undergraduate degree at the [http://biochemistry.utoronto.ca/ University of Toronto in Biochemistry]. She then completed her graduate work supervised by [[User: Lynne Howell|Lynne Howell]] conducting research out of the Hospital for Sick Children. This led to her obtaining her PhD in Biochemistry from the University of Toronto in 2019. Her research focused on the carbohydrate active enzymes involved in exopolysaccharide production used by microbes in biofilm formation. This included structural and biochemical characterization of glycoside hydrolases <cite>Bamford2015 Snarr2017 Little2018 LeMauff2019 Bamford2019</cite>, carbohydrate esterases <cite>Little2014 Little2014b Little2015 Bamford2020</cite>, and a carbohydrate binding module <cite>Bamford2020</cite>. Natalie's studies helped in the creation of three GH families ([[Glycoside Hydrolase Family 135|GH135]], [[Glycoside Hydrolase Family 153|GH153]], [http://www.cazy.org/GH166.html GH166]), one CE family (CE18) and one CBM family ([[Carbohydrate Binding Module Family 87|CBM87]]). She is now a postdoctoral fellow at the University of Dundee with [https://www.lifesci.dundee.ac.uk/people/nicola-stanley-wall Nicola Stanley-Wall].  
  
 
She has aided in the determination of crystal structures including:
 
She has aided in the determination of crystal structures including:

Revision as of 05:43, 29 May 2020

NatalieBamford.png

Natalie Bamford did her undergraduate degree at the University of Toronto in Biochemistry. She then completed her graduate work supervised by Lynne Howell conducting research out of the Hospital for Sick Children. This led to her obtaining her PhD in Biochemistry from the University of Toronto in 2019. Her research focused on the carbohydrate active enzymes involved in exopolysaccharide production used by microbes in biofilm formation. This included structural and biochemical characterization of glycoside hydrolases [1, 2, 3, 4, 5], carbohydrate esterases [6, 7, 8, 9], and a carbohydrate binding module [9]. Natalie's studies helped in the creation of three GH families (GH135, GH153, GH166), one CE family (CE18) and one CBM family (CBM87). She is now a postdoctoral fellow at the University of Dundee with Nicola Stanley-Wall.

She has aided in the determination of crystal structures including:

  • GH114 Aspergillus fumigatus Ega3, an α-1,4-galactosaminidase [5]
  • GH135 Aspergillus clavatus Sph3, an α-1,4-N-acetylgalactosaminidase [1]
  • GH153 Bordetella bronchiseptica PgaB, a poly-β-1,6-D-glucosamine hydrolase [3]
  • CE4 Ammonifex degensii IcaB, a poly-β-1,6-N-acetyl-D-glucosamine deacetylase [7]
  • CE18 and CBM87 Aspergillus fumigatus Agd3, an α-1,4-N-acetylgalactosaminidase deacetylase [9]

  1. pmid:26342082

    [Bamford2015]
  2. pmid:28634301

    [Snarr2017]
  3. pmid:29684093

    [Little2018]
  4. pmid:31167793

    [LeMauff2019]
  5. pmid:31416836

    [Bamford2019]
  6. pmid:24994902

    [Little2014]
  7. pmid:25359777

    [Little2014b]
  8. pmid:26203190

    [Little2015]
  9. pmid:32415073

    [Bamford2020]