Advances in glycosaminoglycanomics by 15N-NMR spectroscopy
Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosami...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Pomin, Vitor H. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag Berlin Heidelberg 2013 |
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| Übergeordnetes Werk: |
Enthalten in: Analytical and bioanalytical chemistry - Berlin : Springer, 2002, 405(2013), 10 vom: 17. Feb., Seite 3035-3048 |
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| Übergeordnetes Werk: |
volume:405 ; year:2013 ; number:10 ; day:17 ; month:02 ; pages:3035-3048 |
| Links: |
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| DOI / URN: |
10.1007/s00216-013-6803-7 |
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SPR002216906 |
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| 520 | |a Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances | ||
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10.1007/s00216-013-6803-7 doi (DE-627)SPR002216906 (SPR)s00216-013-6803-7-e DE-627 ger DE-627 rakwb eng Pomin, Vitor H. verfasserin aut Advances in glycosaminoglycanomics by 15N-NMR spectroscopy 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2013 Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances Amino sugars (dpeaa)DE-He213 Biomolecular NMR (dpeaa)DE-He213 Glycosaminoglycans (dpeaa)DE-He213 N-NMR (dpeaa)DE-He213 Enthalten in Analytical and bioanalytical chemistry Berlin : Springer, 2002 405(2013), 10 vom: 17. Feb., Seite 3035-3048 (DE-627)25372337X (DE-600)1459122-4 1618-2650 nnns volume:405 year:2013 number:10 day:17 month:02 pages:3035-3048 https://dx.doi.org/10.1007/s00216-013-6803-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 405 2013 10 17 02 3035-3048 |
| spelling |
10.1007/s00216-013-6803-7 doi (DE-627)SPR002216906 (SPR)s00216-013-6803-7-e DE-627 ger DE-627 rakwb eng Pomin, Vitor H. verfasserin aut Advances in glycosaminoglycanomics by 15N-NMR spectroscopy 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2013 Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances Amino sugars (dpeaa)DE-He213 Biomolecular NMR (dpeaa)DE-He213 Glycosaminoglycans (dpeaa)DE-He213 N-NMR (dpeaa)DE-He213 Enthalten in Analytical and bioanalytical chemistry Berlin : Springer, 2002 405(2013), 10 vom: 17. Feb., Seite 3035-3048 (DE-627)25372337X (DE-600)1459122-4 1618-2650 nnns volume:405 year:2013 number:10 day:17 month:02 pages:3035-3048 https://dx.doi.org/10.1007/s00216-013-6803-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 405 2013 10 17 02 3035-3048 |
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10.1007/s00216-013-6803-7 doi (DE-627)SPR002216906 (SPR)s00216-013-6803-7-e DE-627 ger DE-627 rakwb eng Pomin, Vitor H. verfasserin aut Advances in glycosaminoglycanomics by 15N-NMR spectroscopy 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2013 Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances Amino sugars (dpeaa)DE-He213 Biomolecular NMR (dpeaa)DE-He213 Glycosaminoglycans (dpeaa)DE-He213 N-NMR (dpeaa)DE-He213 Enthalten in Analytical and bioanalytical chemistry Berlin : Springer, 2002 405(2013), 10 vom: 17. Feb., Seite 3035-3048 (DE-627)25372337X (DE-600)1459122-4 1618-2650 nnns volume:405 year:2013 number:10 day:17 month:02 pages:3035-3048 https://dx.doi.org/10.1007/s00216-013-6803-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 405 2013 10 17 02 3035-3048 |
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10.1007/s00216-013-6803-7 doi (DE-627)SPR002216906 (SPR)s00216-013-6803-7-e DE-627 ger DE-627 rakwb eng Pomin, Vitor H. verfasserin aut Advances in glycosaminoglycanomics by 15N-NMR spectroscopy 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2013 Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances Amino sugars (dpeaa)DE-He213 Biomolecular NMR (dpeaa)DE-He213 Glycosaminoglycans (dpeaa)DE-He213 N-NMR (dpeaa)DE-He213 Enthalten in Analytical and bioanalytical chemistry Berlin : Springer, 2002 405(2013), 10 vom: 17. Feb., Seite 3035-3048 (DE-627)25372337X (DE-600)1459122-4 1618-2650 nnns volume:405 year:2013 number:10 day:17 month:02 pages:3035-3048 https://dx.doi.org/10.1007/s00216-013-6803-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 405 2013 10 17 02 3035-3048 |
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10.1007/s00216-013-6803-7 doi (DE-627)SPR002216906 (SPR)s00216-013-6803-7-e DE-627 ger DE-627 rakwb eng Pomin, Vitor H. verfasserin aut Advances in glycosaminoglycanomics by 15N-NMR spectroscopy 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2013 Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances Amino sugars (dpeaa)DE-He213 Biomolecular NMR (dpeaa)DE-He213 Glycosaminoglycans (dpeaa)DE-He213 N-NMR (dpeaa)DE-He213 Enthalten in Analytical and bioanalytical chemistry Berlin : Springer, 2002 405(2013), 10 vom: 17. Feb., Seite 3035-3048 (DE-627)25372337X (DE-600)1459122-4 1618-2650 nnns volume:405 year:2013 number:10 day:17 month:02 pages:3035-3048 https://dx.doi.org/10.1007/s00216-013-6803-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 405 2013 10 17 02 3035-3048 |
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| author |
Pomin, Vitor H. |
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Pomin, Vitor H. misc Amino sugars misc Biomolecular NMR misc Glycosaminoglycans misc N-NMR Advances in glycosaminoglycanomics by 15N-NMR spectroscopy |
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Advances in glycosaminoglycanomics by 15N-NMR spectroscopy Amino sugars (dpeaa)DE-He213 Biomolecular NMR (dpeaa)DE-He213 Glycosaminoglycans (dpeaa)DE-He213 N-NMR (dpeaa)DE-He213 |
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Advances in glycosaminoglycanomics by 15N-NMR spectroscopy |
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advances in glycosaminoglycanomics by 15n-nmr spectroscopy |
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Advances in glycosaminoglycanomics by 15N-NMR spectroscopy |
| abstract |
Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances © Springer-Verlag Berlin Heidelberg 2013 |
| abstractGer |
Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances © Springer-Verlag Berlin Heidelberg 2013 |
| abstract_unstemmed |
Abstract Recent developments to enhance sensitivity in solution NMR spectroscopy such as the advent and spread of the use of high magnetic fields, cryoprobe technology, isotopic labeling techniques, and new combinations of 2D experiments have pushed the limits in structural NMR analysis of glycosaminoglycans (GAGs). This review is dedicated to the less sensitive 15N isotope of hexosamines rather than the commonly used anomeric and ring 1H and 13C resonances of uronic acids and hexosamines. Given that GAG types are basically classified on the basis of their composing hexosamine types together with variations of their sulfation patterns, and epimerized forms of the adjacent uronic acids, 15N-related NMR studies on native GAGs, oligosaccharides, or the various composing amino sugars have proved to be quite useful in the retrieval of both structural and dynamic information, despite the low number of resultant peaks. This in turn reduces significantly chemical shift degeneracy and at the same time facilitates spin and structural assignments. This review covers the principal contributions made so far by solution 15N-NMR spectroscopy to progress in the structural biology of GAGs in the current glycomics age. FigureGlycosaminoglycans and the typical position of their 1H-15N resonances © Springer-Verlag Berlin Heidelberg 2013 |
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Advances in glycosaminoglycanomics by 15N-NMR spectroscopy |
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https://dx.doi.org/10.1007/s00216-013-6803-7 |
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| score |
7.399928 |