Shear banding in strained semicrystalline polyamide 6 films as revealed by atomic force microscopy: Role of the amorphous phase

2004 ◽  
Vol 42 (4) ◽  
pp. 687-701 ◽  
Author(s):  
V. Ferreiro ◽  
G. Coulon
Wear ◽  
2019 ◽  
Vol 418-419 ◽  
pp. 151-159 ◽  
Author(s):  
Juan F. Gonzalez-Martinez ◽  
Erum Kakar ◽  
Stefan Erkselius ◽  
Nicola Rehnberg ◽  
Javier Sotres

Nanoscale ◽  
2017 ◽  
Vol 9 (36) ◽  
pp. 13707-13716 ◽  
Author(s):  
Anna D. Protopopova ◽  
Rustem I. Litvinov ◽  
Dennis K. Galanakis ◽  
Chandrasekaran Nagaswami ◽  
Nikolay A. Barinov ◽  
...  

High-resolution atomic force microscopy imaging reveals the role of fibrinogen αC regions in the early stages of fibrin self-assembly.


2011 ◽  
Vol 3 (6) ◽  
pp. 702-716 ◽  
Author(s):  
Srinivasan Ramachandran ◽  
Fernando Teran Arce ◽  
Ratnesh Lal

2009 ◽  
Vol 22 (5) ◽  
pp. 347-355 ◽  
Author(s):  
Joshua Strauss ◽  
Nancy A. Burnham ◽  
Terri A. Camesano

COSMOS ◽  
2008 ◽  
Vol 04 (02) ◽  
pp. 173-183
Author(s):  
BOON TEE ONG ◽  
PARAYIL KUMARAN AJIKUMAR ◽  
SURESH VALIYAVEETTIL

The present article reviews the self-assembly of oligopeptides to form nanostructures, both in solution and in solid state. The solution structures of the peptides were examined using circular dichroism and dynamic light scattering. The solid state assembly was examined by adsorbing the peptides onto a mica surface and analyzing it using atomic force microscopy. The role of pH and salt concentration on the peptide self-assembly was also examined. Nanostructures within a size range of 3–10 nm were obtained under different conditions.


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