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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1002/mrc.4757
|2 doi
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|a pubmed24n0950.xml
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|a (NLM)29885093
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Ilgen, Julian
|e verfasserin
|4 aut
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| 245 |
1 |
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|a perfectBASH
|b Band-selective homonuclear decoupling in peptides and peptidomimetics
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 27.08.2019
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|a Date Revised 27.08.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2018 John Wiley & Sons, Ltd.
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|a Band selective techniques offer the highest sensitivity of all pure shift approaches and thus are the best choice for decoupling well-separated 1 H-frequency regions, such as the amide- or the α-proton region of α-peptides. They are inept to fully decouple the amide- and the α-proton region simultaneously, though. Herein, we present a new homonuclear decoupling technique, which extends the capabilities of band selective decoupling using the perfect echo principle. This modification allows a complete backbone decoupling (amide- and α-protons) in peptides and opens band selective homonuclear decoupling to substances with two mutually coupled protons in the spectral range of interest
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a 1H-NMR
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|a 2D NMR
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|a NMR
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|a band-selective homonuclear (BASH) decoupling
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|a full sensitivity
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|a peptides
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|a peptidomimetics
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|a perfect echo
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|a pure shift
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|a Peptidomimetics
|2 NLM
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|a Polymers
|2 NLM
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| 650 |
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|a Cyclosporine
|2 NLM
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| 650 |
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|a 83HN0GTJ6D
|2 NLM
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| 700 |
1 |
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|a Kaltschnee, Lukas
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Thiele, Christina M
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Magnetic resonance in chemistry : MRC
|d 1985
|g 56(2018), 10 vom: 08. Okt., Seite 918-933
|w (DE-627)NLM098179667
|x 1097-458X
|7 nnns
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| 773 |
1 |
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|g volume:56
|g year:2018
|g number:10
|g day:08
|g month:10
|g pages:918-933
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|u http://dx.doi.org/10.1002/mrc.4757
|3 Volltext
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