High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy (Q27642920)

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English	High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy	scientific article

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instance of

scholarly article

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title

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy (English)

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main subject

molecular geometry

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spectroscopy

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NMR spectroscopy

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author

Chris Dobson

series ordinal

5

object named as

Christopher M Dobson

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Christopher Jaroniec

object named as

Christopher P Jaroniec

series ordinal

1

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Cait E. MacPhee

object named as

Cait E MacPhee

series ordinal

2

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Michael T. McMahon

object named as

Michael T McMahon

series ordinal

4

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Robert G. Griffin

series ordinal

6

object named as

Robert G Griffin

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author name string

Vikram S Bajaj

series ordinal

3

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language of work or name

English

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publication date

20 January 2004

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

101

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issue

3

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page(s)

711-6

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cites work

Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

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De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.

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A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

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Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils

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Backbone-dependent rotamer library for proteins. Application to side-chain prediction

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Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril

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The protofilament structure of insulin amyloid fibrils

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Amyloid fibers are water-filled nanotubes

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Structural studies of the scrapie prion protein by electron crystallography

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Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration

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29 September 2017

Biomolecular solid state NMR: advances in structural methodology and applications to peptide and protein fibrils

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Amyloid fibrils from muscle myoglobin

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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

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Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register

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From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

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29 September 2017

Amyloid fibril formation by an SH3 domain

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29 September 2017

Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

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Solid-state NMR studies of the prion protein H1 fragment

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Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

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Refined fibril structures: the hydrophobic core in Alzheimer's amyloid beta-protein and prion as revealed by X-ray diffraction.

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Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro

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Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling

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Frequency selective heteronuclear dipolar recoupling in rotating solids: accurate (13)C-(15)N distance measurements in uniformly (13)C,(15)N-labeled peptides.

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3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C,(15)N-labeled solids.

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PROCHECK: a program to check the stereochemical quality of protein structures

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21 January 2018

Accurate bond and angle parameters for X-ray protein structure refinement

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21 January 2018

Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin.

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21 January 2018

Formation of Mixed Fibrils Demonstrates the Generic Nature and Potential Utility of Amyloid Nanostructures

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21 January 2018

Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron Micrographs

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21 January 2018

The protofilament substructure of amyloid fibrils11Edited by F. E. Cohen

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21 January 2018

Determination of multiple torsion-angle constraints in U-(13)C,(15)N-labeled peptides: 3D (1)H-(15)N-(13)C-(1)H dipolar chemical shift NMR spectroscopy in rotating solids

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X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin

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reference URL

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retrieved

12 December 2020

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inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.0304849101

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ADS bibcode

2004PNAS..101..711J

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Fatcat ID

release_etyv6gjekbexfotscphevyudym

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Fatcat

reference URL

https://api.fatcat.wiki/v0/release/etyv6gjekbexfotscphevyudym

retrieved

24 November 2022

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PMC publication ID

321745

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PubMed publication ID

14715898

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ResearchGate publication ID

8924968

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