Exploration of conformational flexibility and hydrogen bonding of xylosides in different solvents, as a model system for enzyme active site interactions
Ronnols, Jerk ; Manner, Sophie LU ; Siegbahn, Anna LU ; Ellervik, Ulf LU
and Widmalm, Goran
(2013)
In Organic and Biomolecular Chemistry
11(33).
p.5465-5472
- Abstract
- The predominantly populated conformation of carbohydrates in solution does not necessarily represent the biologically active species; rather, any conformer accessible without too large an energy penalty may be present in a biological pathway. Thus, the conformational preferences of a naphthyl xyloside, which initiates in vivo synthesis of antiproliferative glycosaminoglycans, have been studied by using NMR spectroscopy in a variety of solvents. Equilibria comprising the conformations C-4(1), S-2(0) and C-1(4) were found, with a strong dependence on the hydrogen bonding ability of the solvent. Studies of fluorinated analogues revealed a direct hydrogen bond from the hydroxyl group at C2 to the fluorine atom at C4 by a (1h)J(F4,HO2)... (More)
- The predominantly populated conformation of carbohydrates in solution does not necessarily represent the biologically active species; rather, any conformer accessible without too large an energy penalty may be present in a biological pathway. Thus, the conformational preferences of a naphthyl xyloside, which initiates in vivo synthesis of antiproliferative glycosaminoglycans, have been studied by using NMR spectroscopy in a variety of solvents. Equilibria comprising the conformations C-4(1), S-2(0) and C-1(4) were found, with a strong dependence on the hydrogen bonding ability of the solvent. Studies of fluorinated analogues revealed a direct hydrogen bond from the hydroxyl group at C2 to the fluorine atom at C4 by a (1h)J(F4,HO2) coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4025578
- author
- Ronnols, Jerk
; Manner, Sophie
LU
; Siegbahn, Anna
LU
; Ellervik, Ulf
LU
and Widmalm, Goran
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Organic and Biomolecular Chemistry
- volume
- 11
- issue
- 33
- pages
- 5465 - 5472
- publisher
- Royal Society of Chemistry
- external identifiers
-
- wos:000323141800010
- scopus:84881122050
- pmid:23857412
- ISSN
- 1477-0539
- DOI
- 10.1039/c3ob40991k
- language
- English
- LU publication?
- yes
- id
- 94535941-a6f6-4ced-8348-c04526ee8e28 (old id 4025578)
- date added to LUP
- 2016-04-01 10:21:49
- date last changed
- 2024-02-05 03:17:15
@article{94535941-a6f6-4ced-8348-c04526ee8e28,
abstract = {{The predominantly populated conformation of carbohydrates in solution does not necessarily represent the biologically active species; rather, any conformer accessible without too large an energy penalty may be present in a biological pathway. Thus, the conformational preferences of a naphthyl xyloside, which initiates in vivo synthesis of antiproliferative glycosaminoglycans, have been studied by using NMR spectroscopy in a variety of solvents. Equilibria comprising the conformations C-4(1), S-2(0) and C-1(4) were found, with a strong dependence on the hydrogen bonding ability of the solvent. Studies of fluorinated analogues revealed a direct hydrogen bond from the hydroxyl group at C2 to the fluorine atom at C4 by a (1h)J(F4,HO2) coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules.}},
author = {{Ronnols, Jerk and Manner, Sophie and Siegbahn, Anna and Ellervik, Ulf and Widmalm, Goran}},
issn = {{1477-0539}},
language = {{eng}},
number = {{33}},
pages = {{5465--5472}},
publisher = {{Royal Society of Chemistry}},
series = {{Organic and Biomolecular Chemistry}},
title = {{Exploration of conformational flexibility and hydrogen bonding of xylosides in different solvents, as a model system for enzyme active site interactions}},
url = {{http://dx.doi.org/10.1039/c3ob40991k}},
doi = {{10.1039/c3ob40991k}},
volume = {{11}},
year = {{2013}},
}