User:Harry Gilbert - Revision history

Harry Brumer at 16:49, 22 September 2025

2025-09-22T16:49:00Z

Harry Brumer at 14:54, 22 September 2025

2025-09-22T14:54:18Z

Harry Gilbert at 16:18, 30 April 2012

2012-04-30T16:18:16Z

Harry Brumer: standardized picture format

2011-02-08T20:06:31Z

standardized picture format

Harry Gilbert at 11:44, 30 July 2009

2009-07-30T11:44:01Z

Harry Gilbert at 22:09, 28 July 2009

2009-07-28T22:09:17Z

Harry Gilbert at 22:05, 28 July 2009

2009-07-28T22:05:54Z

Harry Gilbert at 21:44, 26 July 2009

2009-07-26T21:44:41Z

Harry Gilbert at 12:03, 23 July 2009

2009-07-23T12:03:45Z

Harry Gilbert at 12:40, 18 June 2009

2009-06-18T12:40:06Z

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-''A true giant in the field, Harry Gilbert passed away in late September, 2025.''  - [[User:Harry Brumer|Harry Brumer]] ([[User talk:Harry Brumer|talk]]) 07:53, 22 September 2025 (PDT)
+''[https://pubmed.ncbi.nlm.nih.gov/?term=gilbert%20HJ&sort=date A true giant in the field], Harry Gilbert passed away in late September, 2025.''  - [[User:Harry Brumer|Harry Brumer]] ([[User talk:Harry Brumer|talk]]) 07:53, 22 September 2025 (PDT)
 [[Category:Contributors|Gilbert, Harry]]

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 After working at Newcastle University since 1985 I moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA, returning to Newcastle University in November 2010. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.
+''A true giant in the field, Harry Gilbert passed away in late September, 2025.''  - [[User:Harry Brumer|Harry Brumer]] ([[User talk:Harry Brumer|talk]]) 07:53, 22 September 2025 (PDT)
 [[Category:Contributors|Gilbert, Harry]]

← Older revision		Revision as of 16:18, 30 April 2012
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	[[Image:gilbert.jpg\|200px\|right]]		[[Image:gilbert.jpg\|200px\|right]]

−	After working at Newcastle University since 1985 I ~~have recently~~ moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.	+	After working at Newcastle University since 1985 I moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA, returning to Newcastle University in November 2010. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.

← Older revision		Revision as of 20:06, 8 February 2011
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−	~~Harry Gilbert~~	+	[[Image:gilbert.jpg\|200px\|right]]
−	[[Image:gilbert.jpg\|right]]

	After working at Newcastle University since 1985 I have recently moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.		After working at Newcastle University since 1985 I have recently moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.

← Older revision		Revision as of 11:44, 30 July 2009
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	Harry Gilbert		Harry Gilbert
	[[Image:gilbert.jpg\|right]]		[[Image:gilbert.jpg\|right]]
		+
		+	After working at Newcastle University since 1985 I have recently moved (November 2008) to the Complex Carbohydrate Research Center at the University of Georgia in Athens, USA. My major research interests are focused on enzymes that modify complex carbohydrates. I am interested in glycoside hydrolases and glycosyltransferases. I also have a generic interest in the mechanism of carbohydrate-protein recognition using non-catalytic carbohydrate binding modules (CBMs) as my model system. My research is focused on understanding the catalytic mechanism and the structural basis for the substrate specificity displayed by these enzymes. We use a combination of structural biology, primarily X-ray crystallography but also NMR, to determine the three dimensional structure of these enzymes, in combination with rational design and forced protein evolution to dissect how these enzymes work.

← Older revision		Revision as of 22:09, 28 July 2009
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	Harry Gilbert		Harry Gilbert
−		+	[[Image:gilbert.jpg\|right]]

← Older revision		Revision as of 22:05, 28 July 2009
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−	~~GH62~~	+	Harry Gilbert
−
−	~~Substrate specificity~~
−	Arabinofuranosidases that specifically cleave either alpha1,2 or alpha1,3 Larabinofuranose sidechains from xylans. The enzyme will not act on xylose moieties in xylan that are decorated at both O2 and O3 with an arabinose side chain
−

← Older revision		Revision as of 21:44, 26 July 2009
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	Substrate specificity		Substrate specificity
−		+	Arabinofuranosidases that specifically cleave either alpha1,2 or alpha1,3 Larabinofuranose sidechains from xylans. The enzyme will not act on xylose moieties in xylan that are decorated at both O2 and O3 with an arabinose side chain

← Older revision		Revision as of 12:03, 23 July 2009
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−	~~GH26~~	+	GH62

−	~~Sunstrate~~ specificity	+	Substrate specificity

← Older revision		Revision as of 12:40, 18 June 2009
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	GH26		GH26

−		+	Sunstrate specificity