| DOI | Resolve DOI: https://doi.org/10.1016/j.pnmrs.2010.07.004 |
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| Author | Search for: Wishart, D.S.1 |
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| Affiliation | - National Research Council of Canada. National Institute for Nanotechnology
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| Format | Text, Article |
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| Subject | Bio-molecular; NMR; Prediction; Protein dynamics; Protein structures; Structure; Chemical shift; Nuclear magnetic resonance; Nuclear magnetic resonance spectroscopy; Proteins; Resonance; Chemical analysis; protein; chemistry; computer program; protein conformation; protein database; protein folding; Databases, Protein; Protein Conformation; Protein Folding; Proteins; Software |
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| Abstract | A review of the Progress in Nuclear Magnetic Resonance Spectroscopy journal discusses the roles that chemical shifts can play in understanding and interpreting protein structure and protein dynamics. The focus of the review is limited primarily to the interpretation of reported peptide and protein chemical shifts, which are diamagnetic and isotropic in character. It is expected that kind of review will help increase the awareness of chemical shifts in the NMR community and that it will clarify certain issues pertaining to chemical shifts in biomolecular NMR. It is expected that it will offer new insights into how chemical shifts can be used in protein NMR and give greater confidence to those spectroscopists who are specifically 'NOE-centric' or those who are relatively new to the field to start routinely using chemical shifts in analyzing their protein structures. |
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| Publication date | 2011 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21271051 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 3403b0e2-bce8-48db-8df3-a31cfacb4c73 |
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| Record created | 2014-03-24 |
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| Record modified | 2020-04-21 |
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