Solid State NMR Studies of Biopolymers

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Solid State NMR to look at Protein Complexes

The content of this volume has been added to the online reference work Encyclopedia of Magnetic Resonance. For further information see Encyclopedia of Magnetic Resonance.

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Solid-state NMR studies of collagen-based parchments and gelatin.

The field of solid state NMR of biological samples [ ssNMR] has blossomed in the past years, and a cohesive overview of the technology is needed for new practitioners in industry and academia. This title provides an overview of Solid State NMR methods for studying structure dynamics and ligand-binding in biopolymers, and offers an overview of RF pulse sequences for various applications, including not only a systematic catalog but also a discussion of theoretical tools for analysis of pulse sequences.

Practical examples of biochemical applications are included, along with a detailed discussion of the many aspects of sample preparation and handling that make spectroscopy on solid proteins successful. The Editors regularly commission new articles and updates of existing articles and so EMR is growing year by year. The EMR Books are intended to be of value and interest to research students, postdoctoral fellows and researchers in hospitals, industry and academia learning about the scientific area in question.

NMR Applications in Biopolymers

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Edited by Anne E. McDermott , Edited by Tatyana Polenova.

Freely available

Structural bound water content was estimated from wideline 1H NMR lineshape and relaxation time measurements. It was found that the relative water content in parchments correlates linearly with 13C MAS linewidths. Its decrease on parchment degradation indicates that structural water molecules are of primary importance in stabilizing higher order collagen structures. Backbone and side chain dynamics of collagen in parchments were compared to those of gelatin based on the 13C dipolar-dephased experiments.


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Carbonyl 13C chemical shift anisotropies were measured to deduce the geometry of the collagen backbone motion.