Walz of the Polypeptides by Mara G. Haseltine

Haseltine on her project:

The inspiration for Waltz of the Polypeptides (2003) comes from one of the smallest muses on the planet, a subject so tiny it can only be seen with an electron microscope. It is a sub-cellular organelle called a rhibosome. Within each cell, ribosomes produce the smallest functional elements in all living organisms, proteins. In Waltz of the Polypeptides the viewer literally walks through the birth of a single protein.

To create this work, Mara G. Haseltine studied the ribosomes and proteins and used accurate molecular renderings of electron microscopic and nuclear magnetic resonance images for her armatures. She manipulated this raw data using a 3-D computer program into a design which kept the integrity of Mother Nature’s form while simultaneously creating a work that was comprehensible and pleasing to its viewers. She then fabricated this design into three-dimensions using computer-driven 5-axis milling and rapid prototyping technologies. The work itself was created to be part of a living landscape inspired by the Zen gardens of Kyoto. Each part of the landscape represents a different part of the cell. Thus, when the viewer experiences Waltz of the Polypeptides, they are fully immersed into a fantastical environment based on a tiny part of the human body.

(h/t Alyson Swimm)

the-bumbling-polypeptide asked:

Hi Brontë! I finally had time to watch Pride and I must say it's one of the best decisions I've made in 2015. The characters were excellently portrayed and the movie directed in such a way that I was never bored. I'm glad that I now know about LGSM and the miners' strike— and my favorite part was the pride parade at the end. Thanks for introducing me to this work of art.

you’re so welcome, i’m so so glad you enjoyed it!!

…forcing the conversion from a constant flow of carbs from “healthy whole grains” and sugars to increasing the enzymatic capacity to oxidize fats does indeed cause several weeks of low energy — but how do we explain the depression, nausea, headaches, lightheadedness, dehydration, emotional outbursts, intensive wheat cravings, bloating, constipation, even intensification of joint pain, effects that are not likely attributable to hypoglycemia or poor mobilization of energy? Delayed ramp-up of fatty acid oxidation is indeed part of the reason for the phenomena of wheat withdrawal, but does not explain all of it.

Most of these phenomena are caused by withdrawal from the gliadin-derived opiates in wheat, the 4- to 5-amino acid long polypeptides that increase appetite and cause addictive eating behaviors. You can actually trigger the syndrome abruptly in someone who is not wheat-free by giving them naloxone or naltrexone, opiate-blocking drugs. Because it is a form of opiate withdrawal, it cannot be entirely avoided with known strategies.

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Sickle-cell anemia is a genetic disease caused by alteration of a single amino acid in the hen1oglobin polypeptide. Which one of the following could cause such a mutation?

A . An error in the translation of hemoglobin
B . Insertion of a single nucleotide into the DNA sequence of the gene encoding hemoglobin
C. A frameshift mutation
D • Alteration of a purine to a pyrimidine base

MyChelle Supreme Polypeptide Age Defense Cream Review

Today I am going to review MyChelle Supreme Polypeptide Cream – £36.00which I have been sent very kindly to review on my blog. This is my very first product from MyChelle I have tried. I have read positive feedbacks about many of MyChelle skincare products on beauty blogs. This cream is recommended for Dry skin and Anti-aging concerns. It has some rich ingredients like coconut oil, olive, mango…

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Gel that heals deep wounds in no time

New York, July 3 (IANS) Researchers have developed a protein-based gel that, when exposed to light, can instantly heal wounds.

It heals wounds by acting as a sealant - sticks to the tissue at the site of injury and create a barrier over a wound.

Besides, it can be incorporated with cells in a dish and then injected to stimulate tissue growth.

“We are engineering strong, elastic materials from proteins, so many tissues within the human body are elastic,” said Nasim Annabi, a co-senior author of the study, from Brigham and Women’s Hospital (BWH) in Boston.

“If we want to use biomaterials to regenerate those tissues, we need elasticity and flexibility. Our hydrogel is very flexible, made from a biocompatible polypeptide and can be activated using light.”

Hydrogels - the jelly-like materials that can mimic the properties of human tissue - are widely used in biomedicine, but currently available materials have limitations.

“Some synthetic gels degrade into toxic chemicals over time, and some natural gels are not strong enough to withstand the flow of arterial blood through them,” said lead researcher Ali Khadem hosseini.

The material, known as a photocrosslinkable elastin-like polypeptide-based (ELP) hydrogel, offers several benefits.

It was possible to combine the gel with silica nanoparticles - microscopic particles previously found to stop bleeding - to develop an even more powerful barrier to promote wound healing.

“This could allow us to immediately stop bleeding with one treatment,” said Annabi.

“We see great potential for use in the clinic. The material is biocompatible, and we hope to see it solve clinical problems in the future.”

This elastic hydrogel is formed by using a light-activated polypeptide. When exposed to light, strong bonds form between the molecules of the gel, providing mechanical stability without the need for any chemical modifiers to be added to the material.

The ELP hydrogel can be digested overtime by naturally-occurring enzymes and does not have toxic effects when tested with living cells in the lab.

They found that they could control how much the material swelled as well as its strength, finding that the ELP hydrogel could withstand more stretching than experienced by arterial tissue in the body.

The results were described in the journal Advanced Functional Materials.

The N terminus of pro-endothelial monocyte-activating polypeptide II (EMAP II) regulates its binding with the C terminus, arginyl-tRNA synthetase, and neurofilament light protein.

Related Articles

The N terminus of pro-endothelial monocyte-activating polypeptide II (EMAP II) regulates its binding with the C terminus, arginyl-tRNA synthetase, and neurofilament light protein.

J Biol Chem. 2015 Apr 10;290(15):9753-66

Authors: Xu H, Malinin NL, Awasthi N, Schwarz RE, Schwarz MA

Pro-endothelial monocyte-activating polypeptide II (EMAP II), one component of the multi-aminoacyl tRNA synthetase complex, plays multiple roles in physiological and pathological processes of protein translation, signal transduction, immunity, lung development, and tumor growth. Recent studies have determined that pro-EMAP II has an essential role in maintaining axon integrity in central and peripheral neural systems where deletion of the C terminus of pro-EMAP II has been reported in a consanguineous Israeli Bedouin kindred suffering from Pelizaeus-Merzbacher-like disease. We hypothesized that the N terminus of pro-EMAP II has an important role in the regulation of protein-protein interactions. Using a GFP reporter system, we defined a putative leucine zipper in the N terminus of human pro-EMAP II protein (amino acid residues 1-70) that can form specific strip-like punctate structures. Through GFP punctum analysis, we uncovered that the pro-EMAP II C terminus (amino acids 147-312) can repress GFP punctum formation. Pulldown assays confirmed that the binding between the pro-EMAP II N terminus and its C terminus is mediated by a putative leucine zipper. Furthermore, the pro-EMAP II 1-70 amino acid region was identified as the binding partner of arginyl-tRNA synthetase, a polypeptide of the multi-aminoacyl tRNA synthetase complex. We also determined that the punctate GFP pro-EMAP II 1-70 amino acid aggregate colocalizes and binds to the neurofilament light subunit protein that is associated with pathologic neurofilament network disorganization and degeneration of motor neurons. These findings indicate the structure and binding interaction of pro-EMAP II protein and suggest a role of this protein in pathological neurodegenerative diseases.

PMID: 25724651 [PubMed - indexed for MEDLINE] http://dlvr.it/BLjwBN

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Viruses, Vol. 7, Pages 3329-3344: Characterisation of Structural Proteins from Chronic Bee Paralysis Virus (CBPV) Using Mass Spectrometry

Chronic bee paralysis virus (CBPV) is the etiological agent of chronic paralysis, an infectious and contagious disease in adult honeybees. CBPV is a positive single-stranded #RNA virus which contains two major viral #RNA fragments. #RNA 1 (3674 nt) and #RNA 2 (2305 nt) encode three and four putative open reading frames (ORFs), respectively. #RNA 1 is thought to encode the viral #RNA-dependent #RNA polymerase (RdRp) since the amino acid sequence derived from ORF 3 shares similarities with the RdRP of families Nodaviridae and Tombusviridae. The genomic organization of CBPV and in silico analyses have suggested that #RNA 1 encodes non-structural proteins, while #RNA 2 encodes structural proteins, which are probably encoded by ORFs 2 and 3. In this study, purified CBPV particles were used to characterize virion proteins by mass spectrometry. Several polypeptides corresponding to proteins encoded by ORF 2 and 3 on #RNA 2 were detected. Their role in the formation of the viral capsid is discussed. http://bit.ly/1BJ9ypo #MDPI