The coexistence of rigid and mobile molecules or molecular segments abounds in biomolecular assemblies. Examples include the carbohydrate-rich cell walls of plants and intrinsically disordered proteins that contain rigid ?-sheet cores. In solid-state nuclear magnetic resonance (NMR) spectroscopy, dipolar polarization transfer experiments are well suited for detecting rigid components, whereas scalar-coupling experiments are well suited for detecting highly mobile components. However, few NMR...
[NMR paper] A unified heteronuclear decoupling picture in solid-state NMR under low radio-frequency amplitude and fast magic-angle-spinning frequency regime.
A unified heteronuclear decoupling picture in solid-state NMR under low radio-frequency amplitude and fast magic-angle-spinning frequency regime.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--publishing.aip.org-sites-default-files-aippub-NLM-scitationblue.jpg Related Articles A unified heteronuclear decoupling picture in solid-state NMR under low radio-frequency amplitude and fast magic-angle-spinning frequency regime.
J Chem Phys. 2019 Apr 14;150(14):144201
Authors: Sharma K, Equbal A, Nielsen NC, Madhu PK
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[NMR thesis] Ionic Motion in Solid Electrolytes: A Solid State NMR Study of Sodium and Lithium in ?-Alumina
Ionic Motion in Solid Electrolytes: A Solid State NMR Study of Sodium and Lithium in ?-Alumina
Highe, Albert John (1981) Ionic Motion in Solid Electrolytes: A Solid State NMR Study of Sodium and Lithium in ?-Alumina. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechTHESIS:03062018-120827730
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03-07-2018 08:13 AM
[NMR paper] Handling the influence of chemical shift in amplitude-modulated heteronuclear dipolar recoupling solid-state NMR.
Handling the influence of chemical shift in amplitude-modulated heteronuclear dipolar recoupling solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--publishing.aip.org-sites-default-files-aippub-NLM-scitationblue.jpg Related Articles Handling the influence of chemical shift in amplitude-modulated heteronuclear dipolar recoupling solid-state NMR.
J Chem Phys. 2016 Sep 07;145(9):094202
Authors: Basse K, Shankar R, Bjerring M, Vosegaard T, Nielsen NC, Nielsen AB
Abstract
We present a...
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[NMR paper] Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
J Am Chem Soc. 2017 Jun 14;
Authors: Good D, Pham C, Jagas J, Lewandowski JR, Ladizhansky V
Abstract
Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude...
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[NMR paper] Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers.
Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers.
Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers.
J Chem Phys. 2013 Aug 28;139(8):084203
Authors: Lu GJ, Opella SJ
Abstract
One of the main applications of solid-state NMR is to study the structure and dynamics of biopolymers, such as membrane proteins, under physiological conditions where the polypeptides undergo global motions as they do in biological membranes. The effects of NMR radiofrequency irradiations on...
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[NMR paper] Detection and characterization of an early folding intermediate of T4 lysozyme using
Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Related Articles Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Biochemistry. 1992 May 26;31(20):4749-56
Authors: Lu J, Dahlquist FW
Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme. In the unfolded state, there is little...
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[NMR paper] Detection and characterization of a folding intermediate in barnase by NMR.
Detection and characterization of a folding intermediate in barnase by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles Detection and characterization of a folding intermediate in barnase by NMR.
Nature. 1990 Aug 2;346(6283):488-90
Authors: Bycroft M, Matouschek A, Kellis JT, Serrano L, Fersht AR
Protein engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild-type and mutant proteins, the sequence and energetics of...
Selective Detection of Intermediate-Amplitude Motion by Solid-State NMR
Linear Mode
