User:Gustav Vaaje-Kolstad - Revision history

Harry Brumer: reformatted picture for consistency with other Contributor pages

2013-07-18T16:28:03Z

reformatted picture for consistency with other Contributor pages

Harry Brumer: added intrawiki links and Contributor tag

2013-07-18T16:26:15Z

added intrawiki links and Contributor tag

Gustav Vaaje-Kolstad at 08:25, 18 July 2013

2013-07-18T08:25:02Z

Gustav Vaaje-Kolstad at 08:22, 18 July 2013

2013-07-18T08:22:51Z

Gustav Vaaje-Kolstad at 08:22, 18 July 2013

2013-07-18T08:22:20Z

Gustav Vaaje-Kolstad at 08:20, 18 July 2013

2013-07-18T08:20:06Z

Gustav Vaaje-Kolstad at 08:17, 18 July 2013

2013-07-18T08:17:09Z

Gustav Vaaje-Kolstad at 08:15, 18 July 2013

2013-07-18T08:15:34Z

Gustav Vaaje-Kolstad at 08:14, 18 July 2013

2013-07-18T08:14:10Z

Gustav Vaaje-Kolstad at 08:12, 18 July 2013

2013-07-18T08:12:54Z

← Older revision		Revision as of 16:28, 18 July 2013
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−	[[Image:GVK_pic.jpeg\|~~thumb\|widthpx~~\| ]]	+	[[Image:GVK_pic.jpeg\|200px\|right]]
	I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family [[GH18]] chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,Vaaje-Kolstad2004-2</cite>. During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family [[GH16]] xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.		I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family [[GH18]] chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,Vaaje-Kolstad2004-2</cite>. During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family [[GH16]] xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.

@@ Line 1: / Line 1: @@
 [[Image:GVK_pic.jpeg|thumb|widthpx| ]]
-I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family GH18 chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,Vaaje-Kolstad2004-2</cite>. During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family GH16 xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.
+I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family [[GH18]] chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,Vaaje-Kolstad2004-2</cite>. During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family [[GH16]] xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.
-In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later  able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work, where I'm primarily involved in the work on the former CBM33 family, now named AA10 <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.
+In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of [[Carbohydrate Binding Module Family 33]]. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later  able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in [[Auxiliary Activity Family 9]] and [[Auxiliary Activity Family 10]]. Recent years we have put a lot of effort in figuring out how these enzymes work, where I'm primarily involved in the work on the former [[CBM33]] family, now named [[AA10]] <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012</cite>.
 <biblio>
 #Vaaje-Kolstad2004-1 pmid=14726210
@@ Line 19: / Line 19: @@
 #Aachmann2012 pmid=23112164
 </biblio>

@@ Line 2: / Line 2: @@
 I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family GH18 chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,Vaaje-Kolstad2004-2</cite>. During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family GH16 xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.
-In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later  able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.
+In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later  able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work, where I'm primarily involved in the work on the former CBM33 family, now named AA10 <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.
 My main scientific interest lies in understanding chitin biology with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.

← Older revision		Revision as of 08:22, 18 July 2013
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	In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.		In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.

−	My main scientific interest lies in understanding ~~the~~ biology ~~of chitin~~ with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.	+	My main scientific interest lies in understanding chitin biology with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.

← Older revision		Revision as of 08:22, 18 July 2013
Line 4:		Line 4:
	In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.		In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.

−	My main scientific interest lies in understanding the biology of chitin ~~turnover~~ with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.	+	My main scientific interest lies in understanding the biology of chitin with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.

@@ Line 2: / Line 2: @@
 I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family GH18 chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,Vaaje-Kolstad2004-2</cite>.During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family GH16 xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.
-In the last year of my PhD period I set my on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and later finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.
+In the last year of my PhD period I set my mind on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and later finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.
 My main scientific interest lies in understanding the biology of chitin turnover with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.

@@ Line 2: / Line 2: @@
 I obtained both my MSc (2001) and PhD (2005) in biochemistry in the group of Vincent Eijsink at the Norwegian University of Life Sciences. The main focus of my PhD project was obtaining a deeper insight into catalysis by family GH18 chitinases by combining mutagenesis, enzymology, structural biology and bioinformatic techniques <cite>Vaaje-Kolstad2004-1,2004-2</cite>.During this period I spent a substantial amount of time in the lab of Daan van Aalten at the Wellcome Trust Center, University of Dundee, Scotland, to learn X-ray crystallography and structural biology in general. After finishing my PhD I obtained a 3 year personal post doc grant of which one year was spent in the lab of Geoff Fincher and Maria Hrmova at the University of Adelaide, Australia, where I studied the role of family GH16 xyloglucan endotransferases (XETs) in plant cell wall remodeling <cite>Vaaje-Kolstad2010-1,Vaaje-Kolstad2010-2</cite>.
-In the last year of my PhD period I set my on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and later finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Wong2012,Aachmann2012,</cite>.
+In the last year of my PhD period I set my on figuring out the role of a apparently non-catalytic protein highly expressed by the Gram negative bacterium ''Serratia marcescens'' during chitin degradation. The name of the protein was CBP21 and it was a member of family 33 of the carbohydrate binding modules. After solving the structure of the protein <cite>Vaaje-Kolstad2005-1</cite> and later finding it able to boost chitin degradation by chitinases <cite>Vaaje-Kolstad2005-2</cite>, we were later able to show that the protein was actually an enzyme cleaving glycosidic bonds of chitin chains by a redox-type mechanism <cite>Vaaje-Kolstad2010-3</cite>. Today, this novel enzyme activity is know as lytic polysaccharide monooxygenase (LPMO) and enzymes harbouring this activity are found in families 9 and 10 of the auxiliary activities (AA). Recent years we have put a lot of effort in figuring out how these enzymes work <cite>Forsberg2011,Vaaje-Kolstad2011,Aachmann2012,</cite>.
 My main scientific interest lies in understanding the biology of chitin turnover with an emphasis on the molecular mechanisms of chitin degradation, especially involving family AA10 LPMOs.
@@ Line 15: / Line 15: @@
 #Vaaje-Kolstad2005-2 pmid=15929981
 #Vaaje-Kolstad2010-3 pmid=20929773
 #Forsberg2011 pmid=21748815
 #Vaaje-Kolstad2011 pmid=22210154
 #Aachmann2012 pmid=23112164
 </biblio>