scholarly journals Effects of N-Terminal Residues on the Assembly of Constrained β-Hairpin Peptides Derived from Aβ

2020 ◽  
Vol 142 (26) ◽  
pp. 11593-11601
Author(s):  
Tuan D. Samdin ◽  
Michał Wierzbicki ◽  
Adam G. Kreutzer ◽  
William J. Howitz ◽  
Mike Valenzuela ◽  
...  
Keyword(s):  
Hairpin Peptides

scholarly journals Time-Resolved Temperature-Jump Ir-Measurements on Beta-Hairpin Peptides with Alternate Cross-Strand Interactions

2014 ◽  
Vol 106 (2) ◽  
pp. 52a
Author(s):  
Alexander Popp ◽  
Ling Wu ◽  
Timothy A. Keiderling ◽  
Karin Hauser
Keyword(s):  
Temperature Jump ◽  
Time Resolved ◽  
Beta Hairpin ◽  
Hairpin Peptides

Insertion of Methylene Units into the Turn Segment of Designed β-Hairpin Peptides

1999 ◽  
Vol 121 (23) ◽  
pp. 5360-5363 ◽  
Author(s):  
S. C. Shankaramma ◽  
S. Kumar Singh ◽  
Aruna Sathyamurthy ◽  
P. Balaram
Keyword(s):  
Hairpin Peptides

Design, expression, and purification of de novo transmembrane “hairpin” peptides

Biopolymers ◽  
2012 ◽  
Vol 98 (6) ◽  
pp. 546-556 ◽  
Author(s):  
David V. Tulumello ◽  
Rachel M. Johnson ◽  
Inga Isupov ◽  
Charles M. Deber
Keyword(s):  
De Novo ◽  
Expression And Purification ◽  
Hairpin Peptides

scholarly journals Structure and Assembly of Designed β-Hairpin Peptides in Crystals as Models for β-Sheet Aggregation†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (7) ◽  
pp. 1832-1846 ◽  
Author(s):  
Subrayashastry Aravinda ◽  
Veldore Vidya Harini ◽  
Narayanaswamy Shamala ◽  
Chittaranjan Das ◽  
Padmanabhan Balaram
Keyword(s):  
Hairpin Peptides ◽  
Β Sheet

PROTEIN FORCE-FIELD PARAMETERS OPTIMIZED WITH THE PROTEIN DATA BANK II: COMPARISONS OF FORCE FIELDS BY FOLDING SIMULATIONS OF SHORT PEPTIDES

2004 ◽  
Vol 03 (03) ◽  
pp. 359-378 ◽  
Author(s):  
YOSHITAKE SAKAE ◽  
YUKO OKAMOTO
Keyword(s):  
Force Field ◽  
Protein Data Bank ◽  
Force Fields ◽  
Data Bank ◽  
Optimization Method ◽  
Short Peptides ◽  
Force Field Parameters ◽  
Hairpin Structures ◽  
Hairpin Peptides ◽  
Folding Simulations

In Paper I of this series, the formulations of the optimization method of existing force-field parameters for protein systems have been presented. We then applied it to five sets of force-field parameters, namely, AMBER parm94, AMBER parm96, AMBER parm99, CHARMM version 22, and OPLS-AA. In order to test the validity of these force fields, the folding simulations of α-helical and β-hairpin peptides have been performed with each of the original and optimized force-field parameters. We found that all five modified force-field parameters gave both α-helical and β-hairpin structures more consistent with the experimental implications than the original force fields.

scholarly journals Designed Hairpin Peptides Interfere with Amyloidogenesis Pathways: Fibril Formation and Cytotoxicity Inhibition, Interception of the Preamyloid State

Biochemistry ◽  
2011 ◽  
Vol 50 (38) ◽  
pp. 8202-8212 ◽  
Author(s):  
Kelly N. L. Huggins ◽  
Marco Bisaglia ◽  
Luigi Bubacco ◽  
Marianna Tatarek-Nossol ◽  
Aphrodite Kapurniotu ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Hairpin Peptides
Sign in / Sign up

Export Citation Format

Share Document