التفاصيل البيبلوغرافية
| العنوان: |
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide |
| المؤلفون: |
Ruben Diaz-avalos, Chris Long, Eric Fontano, Melinda Balbirnie, Robert Grothe, David Eisenberg, Donald L. D. Caspar |
| المساهمون: |
The Pennsylvania State University CiteSeerX Archives |
| المصدر: |
https://www.doe-mbi.ucla.edu/Reprints/222Test Diaz-Avalos, Cross Beta Order and Diversity, JMB 2003.pdf. |
| سنة النشر: |
2003 |
| المجموعة: |
CiteSeerX |
| الوصف: |
The seven-residue peptide GNNQQNY from the N-terminal region of the yeast prion protein Sup35, which forms amyloid fibers, colloidal aggregates and highly ordered nanocrystals, provides a model system for characterizing the elusively protean cross-beta conformation. Depending on preparative conditions, orthorhombic and monoclinic crystals with similar lath-shaped morphology have been obtained. Ultra high-resolution (,0.5 A ˚ spacing) electron diffraction patterns from single nanocrystals show that the peptide chains pack in parallel cross-beta columns with,4.86 A ˚ axial spacing. Mosaic striations 20–50 nm wide observed by electron microscopy indicate lateral size-limiting crystal growth related to amyloid fiber formation. Frequently obtained orthorhombic forms, with apparent space group symmetry P212121; have cell dimensions ranging from lal 22:7 – 21:2 A ˚ , lbl 39:9 – 39:3 A ˚ , lcl 4:89 – 4:86 A for wet to dried states. Electron diffraction data from single nanocrystals, recorded in tilt series of still frames, have been mapped in reciprocal space. However, reliable integrated intensities cannot be obtained from |
| نوع الوثيقة: |
text |
| وصف الملف: |
application/pdf |
| اللغة: |
English |
| العلاقة: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.433.1406Test |
| حقوق: |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
| رقم الانضمام: |
edsbas.CAA4E4A3 |
| قاعدة البيانات: |
BASE |
