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Researchers make nanosheets that mimic protein formation
October 13, 2006
ANN ARBOR, Mich.--How to direct and control the self-assembly of nanoparticles is a fundamental question in nanotechnology. University of Michigan researchers have discovered a way to make nanocrystals in a fluid assemble into free-floating sheets the same way some protein structures form in living organisms.
"This establishes an important connection between two basic building blocks in biology and nanotechnology, that is, proteins and nanoparticles, and this is very exciting for assembling materials from the bottom up for a whole slew of applications ranging from drug delivery to energy," said Sharon Glotzer, professor of chemical engineering and materials science and engineering.
Glotzer and Nicholas Kotov, associate professor of chemical engineering, and their graduate students and post doctoral researchers have co-authored a paper scheduled to appear Oct. 13 in the journal Science.
"The importance of this work is in making a key connection between the world of proteins and the world of nanotechnology" Kotov said. "Once we know how to manipulate the forces between the nanoparticles and their ability to self-organize, it will help us in a variety of practical applications from light-harvesting nanoparticle devices to new drugs which can act like proteins, but are actually nanoparticles."
The sheets, which can appear colored under UV illumination from bright green to dark red depending on the nanoparticle size, are made from cadmium telluride crystals, a material used in solar cells. The sheets are about 2 microns in width, about 1/5 the thickness of a human hair.
Scientists have long known how to coax nanoparticles into forming sheets, Glotzer said. But those sheets have only been achieved when the particles were on a surface or at an interface between two fluids, never while suspended in a single fluid.
The work started in Kotov's lab three years ago, when he and his team observed the sheets in experiments. Though they created them, they weren't sure how.
"We were aware of certain proteins in living organisms that self-assemble into layers, called S-layers," Kotov said. S-layer proteins comprise the outermost cell envelope of a wide variety of bacteria and other single-celled, prokaryotic organisms called archaea, and they are able to form 2-d sheets with square, hexagonal, and other packings at surfaces and interfaces, as well as suspended in fluid. The group sought to make the connection between the forces governing S-layer protein assembly and the forces governing the nanoparticle assembly. That's when Glotzer's group, whose expertise is in computer modeling and simulation, became involved.
"It's likely that the forces between S-layer proteins are highly anisotropic, and we suspected this was also a feature of the nanoparticles," Glotzer said. "Computer simulations allowed us to further develop and test this hypothesis."
Post doctoral researcher Zhenli Zhang of Glotzer's group tried various combinations of forces based on information gleaned from experiments performed by post doctoral Zhiyong Tang of Kotov's group. The team discovered that the unique shape of the CdTe nanocrystals gave rise to a combination of forces that conspired to produce the unusual two-dimensional packing. Subsequent experiments by Kotov's group showed that if any of the forces were missing, the sheets would not form, confirming the simulation predictions.
"Self-assembly is nature's basic building principle for producing organized arrays of biomolecules with controlled geometrical and physicochemical surface properties," Glotzer said. "In the fabrication of functional nanoscale materials and devices, self-assembly offers substantial advantages over traditional manufacturing approaches, if we can design the building blocks appropriately. This is what we're trying to do."
University of Michigan
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Deamidation and Isoaspartate Formation in Peptides and Proteins (Crc Series in Analytical Biotechnology)
by Dana W. Aswad (Editor)
As the biotechnology industry provides an increasing number of protein-based pharmaceuticals, it is important to understand the sources of heterogeneity and instability of purified proteins. Deamidation and Isoaspartate Formation in Peptides and Proteins focuses exclusively on these topics. It provides a comprehensive presentation of the mechanisms and conditions that lead to deamidation and isoaspartate formation, the effect of protein structure on the susceptibility of proteins to these reactions, the functional consequences of these reactions, and methodology that can be used to assess the amount and location of these damage reactions in proteins. The thirteen chapters, all written by highly respected experts, cover general reviews, case studies, and methodology. Numerous tables...
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Vitamin B-12 Sublingual 2000 mcg 50 Tablets
by Source Naturals
Vitamin B-12 is an essential nutrient, involved in protein formation. The coenzyme form of vitamin B-12 is necessary for carbohydrate, protein and fat metabolism, as well as for proper DNA replication. Source Naturals Vitamin B-12 tablets are formulated to dissolve easily under the tongue for more direct absorption into the bloodstream. This minimizes destruction of the vitamin B-12 by stomach acids.
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Fitness Pro L-Glutamine 500 mg 60 caps Strength Energy Enhancer
by Fitness Pro
LGlutamine is known for speeding up muscle recovery, increasing strength and energy enhancement. Glutamine is the most abundant amino acid in muscle tissue and plays a key role in many bodily functions. During stressful situations (i.e. heavy resistive weight training) the body can loose a large amount of Glutamine. A loss of Glutamine during exercise may be a signal for muscle breakdown. Glutamine supplementation has been shown to prevent the loss of body mass through the positive role it plays in protein synthesis and its action as a potent anabolic agent. When muscle Glutamine levels are restored and in a positive nitrogen balance, muscle synthesis can return to a normal rate. Glutamine also has actions on glucose metabolism and the regulation of gluconeogenesis. It converts to glucose...
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An Investigation of Hydrourushiol (PDC) Protein Interactions. Formation and Properties of Various PDQ - Protein and Related Conjugates
by Joseph Stauffer (Author)
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Business Wire : Brain Synapse Formation Linked to Proteins, Stanford Study Finds.
by Business Wire (Publisher)
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Particles at Fluid Interfaces and Membranes, Volume 10: Attachment of Colloid Particles and Proteins to Interfaces and Formation of Two-Dimensional Arrays (Studies in Interface Science)
by P. Kralchevsky (Editor), K. Nagayama (Editor)
In the small world of micrometer to nanometer scale many natural and industrial processes include attachment of colloid particles (solid spheres, liquid droplets, gas bubbles or protein macromolecules) to fluid interfaces and their confinement in liquid films. This may lead to the appearance of lateral interactions between particles at interfaces, or between inclusions in phospholipid membranes, followed eventually by the formation of two-dimensional ordered arrays. The book is devoted to the description of such processes, their consecutive stages, and to the investigation of the underlying physico-chemical mechanisms.
The first six chapters give a concise but informative introduction to the basic knowledge in surface and colloid science, which includes both traditional...
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Bacterial Protein Toxins (Handbook of Experimental Pharmacology) (Volume 145)
by K. Aktories (Editor), I. Just (Editor)
In recent years remarkable progress has been accomplished with respect to our knowledge about bacterial protein toxins. This refers especially to structural aspects of protein toxins but also holds true for genetics, molecular biology and biochemical mechanisms underlying the action of toxins. This volume covers the very current and exciting aspects of up-to-date bacterial toxicology and comprehensively reviews the most important bacterial protein toxins such as the intracellular acting toxins which exhibit enzyme activity, as well as those toxins that interact with cell plasma membranes by damaging the membranes (pore formation) or stimulating cell receptors (superantigens). This is the most current reference work on these important bacterial protein toxins, which are presented from the...
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Foldases Catalyzing the Formation and Isomerization of Disulfide Bonds in Proteins
by Natalya K. Nagradova (Author)
One of the rate-limiting steps in the folding pathways of many secretory proteins is the formation of correct disulfide bonds between cysteine residues. In eukaryotes, both disulfide bond formation and isomerisation which shuffles incorrectly formed disulfides are catalysed by protein disulfide isomerase (PDI), whereas in bacteria these two reactions are catalysed by separate enzymes. Both in eukaryotic and prokaryotic cells the oxidation and isomerisation steps proceed exclusively in extracytoplasmic environments (the lumen of the eukaryotic endoplasmic reticulum and the Gram-negative bacterial periplasmic space). The family of foldases under discussion is characterised by a conserved 'thioredoxin fold' and a common active site motif: Cys-X-X-Cys. The process of disulfide bond formation...
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Tumor Formation via Loss of a Molecular Motor Protein [A short communication from: Current Biology
by M. Mazumdar (Author), J.H. Lee (Author), K. Sengupta (Author), T. Ried (Author), Rane (Author)
This digital document is a journal article from Current Biology, published by Elsevier in 2006. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Abstract: Aneuploidy has long been suggested to be causal in tumor formation. Direct testing of this hypothesis has been difficult because of the absence of methods to specifically induce aneuploidy. The chromosome-associated kinesin motor KIF4 plays multiple roles in mitosis, and its loss leads to multiple mitotic defects including aneuploidy [1-5]. Here, we have taken advantage of the direct formation of aneuploidy in the absence of KIF4 to determine whether loss of a molecular motor and generation of aneuploidy during mitosis...
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Foods that fight osteoporosis: certain nutrients like protein, calcium and vitamin D support bone formation, while others can contribute to bone loss.(BONE ... An article from: Women's Health Advisor
by Unavailable (Author)
This digital document is an article from Women's Health Advisor, published by Belvoir Media Group, LLC on September 1, 2009. The length of the article is 967 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available immediately after purchase. You can view it with any web browser.
Citation Details Title: Foods that fight osteoporosis: certain nutrients like protein, calcium and vitamin D support bone formation, while others can contribute to bone loss.(BONE HEALTH) Author: Unavailable Publication: Women's Health Advisor (Magazine/Journal) Date: September 1, 2009 Publisher: Belvoir Media Group, LLC Volume: 13 Issue: 9 Page: 1(2)
Distributed by Gale, a part of Cengage...
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