scholarly journals Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR

2015 ◽  
Vol 119 (47) ◽  
pp. 14892-14904 ◽  
Author(s):  
Liliya Vugmeyster ◽  
Dmitry Ostrovsky ◽  
Toni Villafranca ◽  
Janelle Sharp ◽  
Wei Xu ◽  
...  
Keyword(s):  
Solid State ◽  
Hydrophobic Core ◽  
Deuteron Nmr

scholarly journals Slow Motions in the Hydrophobic Core of Chicken Villin Headpiece Subdomain and Their Contributions to Configurational Entropy and Heat Capacity from Solid-State Deuteron NMR Measurements

Biochemistry ◽  
2011 ◽  
Vol 50 (49) ◽  
pp. 10637-10646 ◽  
Author(s):  
Liliya Vugmeyster ◽  
Dmitry Ostrovsky ◽  
Anastasia Khadjinova ◽  
Jeremy Ellden ◽  
Gina L. Hoatson ◽  
...  
Keyword(s):  
Heat Capacity ◽  
Solid State ◽  
Configurational Entropy ◽  
Hydrophobic Core ◽  
Villin Headpiece ◽  
Slow Motions ◽  
Deuteron Nmr

scholarly journals Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR

2015 ◽  
Vol 1 (11) ◽  
pp. e1501087 ◽  
Author(s):  
Chaowei Shi ◽  
Pascal Fricke ◽  
Lin Lin ◽  
Veniamin Chevelkov ◽  
Melanie Wegstroth ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Caulobacter Crescentus ◽  
Heavy Atom ◽  
Cytoskeletal Proteins ◽  
Atomic Resolution ◽  
Hydrophobic Core ◽  
X Ray Crystallography ◽  
Wide Range ◽  
Resolution Structure

Bactofilins are a recently discovered class of cytoskeletal proteins of which no atomic-resolution structure has been reported thus far. The bacterial cytoskeleton plays an essential role in a wide range of processes, including morphogenesis, cell division, and motility. Among the cytoskeletal proteins, the bactofilins are bacteria-specific and do not have a eukaryotic counterpart. The bactofilin BacA of the speciesCaulobacter crescentusis not amenable to study by x-ray crystallography or solution nuclear magnetic resonance (NMR) because of its inherent noncrystallinity and insolubility. We present the atomic structure of BacA calculated from solid-state NMR–derived distance restraints. We show that the core domain of BacA forms a right-handed β helix with six windings and a triangular hydrophobic core. The BacA structure was determined to 1.0 Å precision (heavy-atom root mean square deviation) on the basis of unambiguous restraints derived from four-dimensional (4D) HN-HN and 2D C-C NMR spectra.

scholarly journals Dynamics of Serine-8 Side-Chain in Amyloid-β Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR

2020 ◽  
Vol 124 (23) ◽  
pp. 4723-4731
Author(s):  
Liliya Vugmeyster ◽  
Dan Fai Au ◽  
Dmitry Ostrovsky ◽  
Dillon Ray Lee Rickertsen ◽  
Scott M. Reed
Keyword(s):  
Amino Acid ◽  
Solid State ◽  
Amyloid Β ◽  
Side Chain ◽  
Deuteron Nmr

scholarly journals Solid-State NMR Reveals the Hydrophobic-Core Location of Poly(amidoamine) Dendrimers in Biomembranes

2010 ◽  
Vol 132 (23) ◽  
pp. 8087-8097 ◽  
Author(s):  
Pieter E. S. Smith ◽  
Jeffrey R. Brender ◽  
Ulrich H. N. Dürr ◽  
Jiadi Xu ◽  
Douglas G. Mullen ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Hydrophobic Core

scholarly journals Structure and Orientation of Pardaxin Determined by NMR Experiments in Model Membranes

2004 ◽  
Vol 279 (44) ◽  
pp. 45815-45823 ◽  
Author(s):  
Fernando Porcelli ◽  
Bethany Buck ◽  
Dong-Kuk Lee ◽  
Kevin J. Hallock ◽  
Ayyalusamy Ramamoorthy ◽  
...  
Keyword(s):  
Solid State ◽  
Lipid Bilayers ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Double Resonance ◽  
Slow Motion ◽  
Solution Nmr ◽  
Helical Conformation ◽  
Hydrophobic Core ◽  
Nmr Studies

Pardaxins are a class of ichthyotoxic peptides isolated from fish mucous glands. Pardaxins physically interact with cell membranes by forming pores or voltage-gated ion channels that disrupt cellular functions. Here we report the high-resolution structure of synthetic pardaxin Pa4 in sodium dodecylphosphocholine micelles, as determined by1H solution NMR spectroscopy. The peptide adopts a bend-helix-bend-helix motif with an angle between the two structure helices of 122 ± 9°, making this structure substantially different from the one previously determined in organic solvents. In addition, paramagnetic solution NMR experiments on Pa4 in micelles reveal that except for the C terminus, the peptide is not solvent-exposed. These results are complemented by solid-state NMR experiments on Pa4 in lipid bilayers. In particular,13C-15N rotational echo double-resonance experiments in multilamellar vesicles support the helical conformation of the C-terminal segment, whereas2H NMR experiments show that the peptide induces considerable disorder in both the head-groups and the hydrophobic core of the bilayers. These solid-state NMR studies indicate that the C-terminal helix has a transmembrane orientation in DMPC bilayers, whereas in POPC bilayers, this domain is heterogeneously oriented on the lipid surface and undergoes slow motion on the NMR time scale. These new data help explain how the non-covalent interactions of Pa4 with lipid membranes induce a stable secondary structure and provide an atomic view of the membrane insertion process of Pa4.

Solid State Deuteron NMR Studies of Polyamidoamine Dendrimer Salts. 2. Relaxation and Molecular Motion

2000 ◽  
Vol 33 (20) ◽  
pp. 7508-7520 ◽  
Author(s):  
Dariya I. Malyarenko ◽  
Robert L. Vold ◽  
Gina L. Hoatson
Keyword(s):  
Solid State ◽  
Molecular Motion ◽  
Nmr Studies ◽  
Polyamidoamine Dendrimer ◽  
Deuteron Nmr

Dynamic study of poly(styrene-vinyl-d3) in a glassy blend by two-dimensional solid-state deuteron NMR

1993 ◽  
Vol 26 (20) ◽  
pp. 5372-5378 ◽  
Author(s):  
Y. H. Chin ◽  
P. T. Inglefield ◽  
A. A. Jones
Keyword(s):  
Solid State ◽  
Dynamic Study ◽  
Two Dimensional ◽  
Deuteron Nmr

Shaped Pulses for Selective Inversion in Solid-State Deuteron NMR Spectroscopy

1996 ◽  
Vol 122 (2) ◽  
pp. 165-178 ◽  
Author(s):  
Marco J. Brown ◽  
Gina L. Hoatson ◽  
Robert L. Vold
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Selective Inversion ◽  
Deuteron Nmr
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