scholarly journals Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

10.3791/1032 ◽  
2008 ◽  
Author(s):  
Helgi Ingolfson ◽  
Ruchi Kapoor ◽  
Shemille A. Collingwood ◽  
Olaf Sparre Andersen
Keyword(s):  
Elastic Properties ◽  
Single Molecule

Single-Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

2007 ◽  
pp. 543-570 ◽  
Author(s):  
Olaf S. Andersen ◽  
Michael J. Bruno ◽  
Haiyan Sun ◽  
Roger E. Koeppe
Keyword(s):  
Elastic Properties ◽  
Single Molecule

Single-Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

2007 ◽  
pp. 543-570 ◽  
Author(s):  
Olaf S. Andersen ◽  
Michael J. Bruno ◽  
Haiyan Sun ◽  
Roger E. Koeppe
Keyword(s):  
Elastic Properties ◽  
Single Molecule

Elastic Properties of Nucleic Acids by Single-Molecule Force Spectroscopy

2016 ◽  
Vol 45 (1) ◽  
pp. 65-84 ◽  
Author(s):  
Joan Camunas-Soler ◽  
Marco Ribezzi-Crivellari ◽  
Felix Ritort
Keyword(s):  
Nucleic Acids ◽  
Elastic Properties ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy

scholarly journals Single-molecule lamellar hydrogels from bolaform microbial glucolipids

Soft Matter ◽  
2020 ◽  
Vol 16 (10) ◽  
pp. 2528-2539 ◽  
Author(s):  
Ghazi Ben Messaoud ◽  
Patrick Le Griel ◽  
Sylvain Prévost ◽  
Daniel Hermida-Merino ◽  
Wim Soetaert ◽  
...  
Keyword(s):  
Elastic Properties ◽  
Single Molecule ◽  
Room Temperature ◽  
Ph Sensitive ◽  
Gelling Agent ◽  
Microbial Fermentation

A biobased pH-sensitive glycolipid derived from microbial fermentation spontaneously forms lamellar hydrogels at room temperature and pH < 8 without any gelling agent. The elastic properties derive from interconnected defectuous lamellar domains.

Determining the elastic properties of aptamer-ricin single molecule multiple pathway interactions

2014 ◽  
Vol 104 (19) ◽  
pp. 193702 ◽  
Author(s):  
Bin Wang ◽  
Bosoon Park ◽  
Yongkuk Kwon ◽  
Bingqian Xu
Keyword(s):  
Elastic Properties ◽  
Single Molecule ◽  
Multiple Pathway

Electron Microscopy and image reconstruction reveal the structural basis for spectrin's elastic properties

1992 ◽  
Vol 50 (1) ◽  
pp. 510-511
Author(s):  
Amy M. McGough ◽  
Robert Josephs
Keyword(s):  
Electron Microscopy ◽  
Elastic Properties ◽  
Conformational Changes ◽  
Quaternary Structure ◽  
Three Dimensional ◽  
Membrane Skeleton ◽  
Projection Algorithm ◽  
Structural Basis ◽  
Iterative Approximation ◽  
Membrane Skeletons

The remarkable deformability of the erythrocyte derives in large part from the elastic properties of spectrin, the major component of the membrane skeleton. It is generally accepted that spectrin's elasticity arises from marked conformational changes which include variations in its overall length (1). In this work the structure of spectrin in partially expanded membrane skeletons was studied by electron microscopy to determine the molecular basis for spectrin's elastic properties. Spectrin molecules were analysed with respect to three features: length, conformation, and quaternary structure. The results of these studies lead to a model of how spectrin mediates the elastic deformation of the erythrocyte.Membrane skeletons were isolated from erythrocyte membrane ghosts, negatively stained, and examined by transmission electron microscopy (2). Particle lengths and end-to-end distances were measured from enlarged prints using the computer program MACMEASURE. Spectrin conformation (straightness) was assessed by calculating the particles’ correlation length by iterative approximation (3). Digitised spectrin images were correlation averaged or Fourier filtered to improve their signal-to-noise ratios. Three-dimensional reconstructions were performed using a suite of programs which were based on the filtered back-projection algorithm and executed on a cluster of Microvax 3200 workstations (4).

The method of replication affects metal film granularity and resolution

1989 ◽  
Vol 47 ◽  
pp. 708-709
Author(s):  
George C. Ruben
Keyword(s):  
Electron Beam ◽  
High Resolution ◽  
Film Thickness ◽  
Single Molecule ◽  
Metal Film ◽  
Vertical Surface ◽  
High Resolution Imaging ◽  
Controllable Factors ◽  
Resolution Imaging

Single molecule resolution in electron beam sensitive, uncoated, noncrystalline materials has been impossible except in thin Pt-C replicas ≤ 150Å) which are resistant to the electron beam destruction. Previously the granularity of metal film replicas limited their resolution to ≥ 20Å. This paper demonstrates that Pt-C film granularity and resolution are a function of the method of replication and other controllable factors. Low angle 20° rotary , 45° unidirectional and vertical 9.7±1 Å Pt-C films deposited on mica under the same conditions were compared in Fig. 1. Vertical replication had a 5A granularity (Fig. 1c), the highest resolution (table), and coated the whole surface. 45° replication had a 9Å granulartiy (Fig. 1b), a slightly poorer resolution (table) and did not coat the whole surface. 20° rotary replication was unsuitable for high resolution imaging with 20-25Å granularity (Fig. 1a) and resolution 2-3 times poorer (table). Resolution is defined here as the greatest distance for which the metal coat on two opposing faces just grow together, that is, two times the apparent film thickness on a single vertical surface.

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