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Protein structure in anisotropic environments: Unique structural fold from orientational constraints

✍ Scribed by Quine, J. R. ;Cross, T. A.

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
191 KB
Volume
12
Category
Article
ISSN
1043-7347

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✦ Synopsis

The mathematical foundation of the determination of protein structure from orientational constraints is described. The tools used are vector algebra, gram matrices, and determinants. The discussion begins in the general abstract setting and proceeds to a discussion of how the methods can be applied to the determination of protein structure using solid state nuclear magnetic resonance. Examples are given relating to the structure of the peptide gramicidin A.

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Protein structure in anisotropic environ
Protein structure in anisotropic environments: Development of orientational constraints
✍ Cross, T. A. ;Quine, J. R. πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 246 KB πŸ‘ 1 views

Solid state nuclear magnetic resonance has the potential to characterize membrane protein structures at very high resolution. This paper focuses on the use of orientational constraints for this purpose. These constraints are based on observing the orientation dependence of nuclear spin interactions.

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## Abstract Protein structure determination by solid‐state NMR of aligned samples relies on the fundamental characteristics of the anisotropic nuclear spin interactions present in isotopically labeled proteins. Progress in the implementation of algorithms that calculate protein structures from the

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Residual dipolar couplings for pairs of proximate magnetic nuclei in macromolecules can easily be measured using high-resolution NMR methods when the molecules are dissolved in dilute liquid crystalline media. The resulting couplings can in principle be used to constrain the relative orientation of