Nano-structure and properties of maize zein studied by atomic force microscopy

2005 ◽  
Vol 41 (3) ◽  
pp. 277-281 ◽  
Author(s):  
Yunchang Guo ◽  
Zhongdong Liu ◽  
Hongjie An ◽  
Minqian Li ◽  
Jun Hu
Keyword(s):  
Atomic Force Microscopy ◽  
Structure And Properties ◽  
Nano Structure ◽  
Force Microscopy ◽  
Atomic Force

Structure and Properties of Murine and Human Dentin

2005 ◽  
Vol 874 ◽  
Author(s):  
Stefan Habelitz ◽  
Shabnam Zartoshtimanesh ◽  
Mehdi Balooch ◽  
Sally J. Marshall ◽  
Grayson W. Marshall ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Elastic Modulus ◽  
Dynamic Stiffness ◽  
Model System ◽  
Structure And Properties ◽  
Force Microscopy ◽  
Dental Tissues ◽  
Atomic Force ◽  
Main Structural Feature ◽  
Human Dentin

AbstractMice are commonly considered the model mammal for many biomedical studies. In this work, mouse and human dentin were compared to specify structural and mechanical differences to establish a baseline for comparison of dental tissues between these species. Atomic force microscopy revealed tubules of about 1.0 to 1.6 μm in diameter as the main structural feature in dentin of both species. Nanoindentation yielded the elastic modulus about 15% lower in murine intertubular dentin while the hardness was almost equal. Dynamic stiffness mapping confirmed the lower elastic properties and also revealed that the peritubular region of increased mineralization around tubules is drastically reduced or maybe absent in murine dentin of this age. This study suggests that structural and mechanical differences need to be considered when murine dentin is used as a model system.

scholarly journals Nonlocality Effect in Atomic Force Microscopy Measurement and Its Reduction by an Approaching Method

2005 ◽  
Vol 127 (4) ◽  
pp. 444-450 ◽  
Author(s):  
Ming Hu ◽  
Haiying Wang ◽  
Mengfen Xia ◽  
Fujiu Ke ◽  
Yilong Bai
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Morphology ◽  
Intermolecular Interaction ◽  
Characteristic Size ◽  
Nano Structure ◽  
Force Microscopy ◽  
Atomic Force ◽  
Interaction Distance ◽  
Geometric Size ◽  
Nonlocality Effect

In AFM measurements of surface morphology, the locality is a traditional assumption, i.e., the load recorded by AFM is simply the function of the distance between the tip of AFM and the point on a sample right opposite the tip [Giessibl, F. J., 2003, “Advances in Atomic Force Microscopy,” Rev. Mod. Phys., 75, pp. 949–983]. This paper presents that nonlocality effect may play an important role in atomic force microscopic (AFM) measurement. The nonlocality of AFM measurement results from two different finite scales: the finite scale of the characteristic intermolecular interaction distance and the geometric size of AFM tip. With a coupled molecular-continuum method, we analyzed this nonlocality effect in detail. It is found that the nonlocality effect can be formulated by a few dimensionless parameters characterizing the ratio of the following scales: the characteristic intermolecular interaction distance between the AFM tip and the sample, the characteristic size of the tip and the characteristic nano-structure and∕or the nanoscale roughness on the surface of a sample. The present work also suggests a data processing algorithm—the approaching method, which can reduce the nonlocality effect in AFM measurement of surface morphology effectively.

Three Dimensional Structure of Human Fibrinogen under Aqueous Conditions Visualized by Atomic Force Microscopy

1997 ◽  
Vol 77 (06) ◽  
pp. 1048-1051 ◽  
Author(s):  
Roger E Marchant ◽  
Matthew D Barb ◽  
John R Shainoff ◽  
Steven J Eppell ◽  
David L Wilson ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Three Dimensional ◽  
Hydrophobic Surface ◽  
Dimensional Structure ◽  
Structure And Properties ◽  
Human Fibrinogen ◽  
Force Microscopy ◽  
Atomic Force ◽  
Molecular Scale ◽  
Aqueous Conditions

SummaryFibrinogen plays a central role in surface-induced thrombosis. However, the interactions of fibrinogen with different substrata remain poorly understood because of the difficulties involved in imaging globular proteins under aqueous conditions. We present detailed three dimensional molecular scale images of fibrinogen molecules on a hydrophobic surface under aqueous conditions obtained by atomic force microscopy. Hydrated fibrinogen monomers are visualized as overlapping ellipsoids; dimers and trimers have linear conformations predominantly, and increased affinity for the hydrophobic surface compared with monomeric fibrinogen. The results demonstrate the importance of hydration on protein structure and properties that affect surface-dependent interactions.

Sign in / Sign up

Export Citation Format

Share Document