Structure Determination of Membrane Peptides and Proteins by Solid-State NMR

Kawamura, Izuru; Norisada, Kazushi; Naito, Akira

doi:10.1007/978-981-10-5966-7_9

Cited by 1 publication

(2 citation statements)

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“…3). The 13 C- 15 N internuclear distances were evaluated by analyzing the plot of S/S 0 against NcTr (Equation ( 1)) [21]. The distance between Leu1[ 13 C]-Ala5[ 15 N] and Leu15[ 13 C]-Ala19[ 15 N] was found to be 4.6 Å and 4.5 Å, respectively.…”

Section: Secondary Structures Of α3 and Their Orientationmentioning

confidence: 99%

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Structural Analyses of Designed α-Helix and β-Sheet Peptide Nanofibers Using Solid-State Nuclear Magnetic Resonance and Cryo-Electron Microscopy and Introduction of Structure-Based Metal-Responsive Properties

Nakagawa,

Kurokawa,

Kambara

et al. 2024

IJMS

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The 21-residue peptide α3, which is artificially designed and consists of three repeats of 7 residues, is known to rapidly assemble into the α-helix nanofiber. However, its molecular structure within the fiber has not yet been fully elucidated. Thus, we conducted a thorough investigation of the fiber’s molecular structure using solid-state NMR and other techniques. The molecules were found to be primarily composed of the α-helix structure, with some regions near the C- and N-terminal adopting a 310-helix structure. Furthermore, it was discovered that β-sheet hydrogen bonds were formed between the molecules at both ends. These intermolecular interactions caused the molecules to assemble parallelly in the same direction, forming helical fibers. In contrast, we designed two molecules, CaRP2 and βKE, that can form β-sheet intermolecular hydrogen bonds using the entire molecule instead of just the ends. Cryo-EM and other measurements confirmed that the nanofibers formed in a cross β structure, albeit at a slow rate, with the formation times ranging from 1 to 42 days. To create peptide nanofibers that instantaneously respond to changes in the external environment, we designed several molecules (HDM1-3) based on α3 by introducing metal-binding sites. One of these molecules was found to be highly responsive to the addition of metal ions, inducing α-helix formation and simultaneously assembling into nanofibers. The nanofibers lost their structure upon removal of the metal ion. The change occurred promptly and was reversible, demonstrating that the intended level of responsiveness was attained.

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Section: Secondary Structures Of α3 and Their Orientationmentioning

confidence: 99%

“…Two methods of solid-state NMR spectroscopy, 13C CP-MAS (Cross Polarization-Magic Angle Spinning) and REDOR (Rotational Echo Double Resonance), were employed [21]. The former was used to identify the secondary structures of each 13C-labeled sample, while the latter was used to determine the distance between specific atoms.…”

Section: Solid-state Nmr Measurementmentioning

confidence: 99%