Determination of Peptide Amide Configuration in a Model Amyloid Fibril by Solid-State NMR-Reference-Cited by-同舟云学术

Determination of Peptide Amide Configuration in a Model Amyloid Fibril by Solid-State NMR

Published:1997-10-01 Issue:43 Volume:119 Page:10487-10493
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Costa P. R.¹,Kocisko D. A.¹,Sun B. Q.¹,Lansbury, P. T.¹,Griffin R. G.¹

Affiliation:

1. Contribution from the Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, and the Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja971494b

Reference40 articles.

1. An investigation of the structure of silk fibroin

2. X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS

3. The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

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