To install click the Add extension button. That's it.

The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.

4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
Live Statistics
English Articles
Improved in 24 Hours
Added in 24 Hours
What we do. Every page goes through several hundred of perfecting techniques; in live mode. Quite the same Wikipedia. Just better.
.
Leo
Newton
Brights
Milds

George Huntly Lorimer

From Wikipedia, the free encyclopedia

George Lorimer

Born
George Huntly Lorimer

(1942-10-14) October 14, 1942 (age 81)[1]
EducationGeorge Watson's College[1]
Alma mater
AwardsHumboldt Prize (1997)
Scientific career
InstitutionsUniversity of Maryland
ThesisThe role of oxygen in photorespiration (1972)
Websitewww.chem.umd.edu/faculty-staff-directory/facultydirectory/george-lorimer

George Huntly Lorimer (born 1942)[1] FRS[2] is a professor in the Department of Chemistry and Biochemistry at the University of Maryland.[1][3]

Career and research

Lorimer is recognized for his work on mechanism of two proteins, RuBisCO and the GroE chaperonins. Rubisco is the enzyme responsible for photosynthetic carbon fixation, and the GroE chaperonins enable the Adenosine triphosphate (ATP)-dependent folding of many other proteins.[2]

Using Oxygen-18 Lorimer demonstrated the oxygenase activity of RuBisCO, both in vivo and in vitro.[2] He further established the novel mechanism for the activation of RuBisCO by carbon dioxide, the formation of a lysyl-carbamate in the active site.[2] With his colleagues at DuPont he employed chemical quench and other techniques to trap and identify the 6-carbon reaction intermediate of the carboxylation reaction and defined the complete stereo-chemical course of the reaction.[2]

In 1989, using an unequivocally unfolded protein and the purified chaperonin proteins GroEL and GroES, his group was the first to demonstrate the ATP-dependent folding of RuBisCO and many other proteins.[2] With Devarajan (Dave) Thirumalai he performed a bioinformatic analysis to define the structural elements of the substrate proteins that GroEL recognizes.[2] Lorimer has also shown that GroEL can perform work on substrate protein during allosteric transitions. He has determined the crystal structure of the functional form, the symmetric GroEL:GroES2 “football” and established that the GroEL rings operate as parallel-processing, iterative annealing machines.[2]

Awards and honors

Lorimer is a member of the National Academy of Sciences of the United States and a Fellow of the Royal Society (FRS) of London.[2] He was awarded the Humboldt Prize in 1997.[3]

References

  1. ^ a b c d Anon (2017). "Lorimer, Prof. George Huntly". Who's Who (online Oxford University Press ed.). Oxford: A & C Black. doi:10.1093/ww/9780199540884.013.24943. (Subscription or UK public library membership required.)
  2. ^ a b c d e f g h i Anon (1986). "Professor George Lorimer FRS". royalsociety.org. Royal Society. Archived from the original on 2016-04-10. One or more of the preceding sentences incorporates text from the royalsociety.org website where:

    “All text published under the heading 'Biography' on Fellow profile pages is available under Creative Commons Attribution 4.0 International License.” --"Royal Society Terms, conditions and policies". Archived from the original on 2016-11-11. Retrieved 2016-03-09.{{cite web}}: CS1 maint: bot: original URL status unknown (link)

  3. ^ a b "Department of Chemistry and Biochemistry – University of Maryland, College Park MD George Lorimer - Department of Chemistry and Biochemistry". www.chem.umd.edu. Archived from the original on 2017-09-28.

 This article incorporates text available under the CC BY 4.0 license.

This page was last edited on 15 August 2023, at 13:58
Basis of this page is in Wikipedia. Text is available under the CC BY-SA 3.0 Unported License. Non-text media are available under their specified licenses. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc. WIKI 2 is an independent company and has no affiliation with Wikimedia Foundation.