X-Message-Number: 32501 From: "Jens Rabis" <> References: <> Subject: #32497: Translation of German glassy protein paper [RAMole] Date: Mon, 22 Mar 2010 12:01:03 +0100 Hi RAMole, thanks :-) Here is the direct comparison of "Google-Translation" and "Babel Fish". Translated into English was the German link: http://www.scienceticker.info/2010/03/19/protein-zu-glasperlen/ http://translate.google.de/# An elegant method for the preservation of proteins, American researchers have developed. By tiny drops of a protein solution into a liquid desiccant type, transforming the droplets into beads of glass protein. Image: Deborah Rickard, Pratt School of Engineering, Duke University "This protein is non-crystalline glass," said David Needham of Duke University, "it is rather a frozen liquid." Unlike in a crystal, the molecules are not arranged in a glass lined up in formation. Apparently, the dehydration successes so fast that the relatively large protein molecules can not slip into a crystal lattice. In their experiments, Needham and colleagues appeared a thin pipette tip in decanol, a relative of the long-chain alcohol drinking ethanol. Then they pressed a tiny drop of protein solution from the tip. Within a short time that went into the protein solution contained in the alcohol over water. Leaving behind a few hundredths of a millimeter large pearl pure protein, the researchers report in the "Biophysical Journal. The process works so carefully that in glass convicted enzymes after re-addition of water are again operational, initial tests showed four different proteins. The reason for this is likely to pass only the water molecules in the vicinity of the proteins in the alcohol. Those water molecules that are embedded in the structure of large protein molecules, however, remain in place. For microbes is not this "structural water" accessible, so that the protein glass does not constitute a breeding ground for bacteria or fungi, said Needham colleague David Gaul. In addition, protein glass is easier to produce and easier to use as a freeze-injected protein and could, for example in the case of therapeutic proteins directly into the body. A patent for their technique, the researchers have applied already. Research: Deborah L. Rickard, P. Brent Duncan, David Gaul and David Needham, Department of Mechanical Engineering and Materials Science, Duke University, Durham, North Carolina Publication Biophysical Journal, Vol 98 (6), pp 1075-84, DOI 10.1016/j.bpj.2009.11.043 http://babelfish.yahoo.com/ American researchers developed an elegant method for the preservation of proteins. By giving tiny drops to a protein solution to a liquid desiccator, the droplets transform into beads from protein glass. Picture: Deborah Rickard, Pratt School OF engineering, Duke University "This protein glass is not crystalline", explains David Needham of the Duke University, "it is rather a rigid liquid." Differently than in a crystal, the molecules are in a glass not in line up and member arranged. Obviously take place the dehydration so rapidly that the comparatively large protein molecules no more could not slip into a crystal lattice. With their experiments Needham and colleagues dipped a thin pipette point into Dekanol, langkettigen relatives of the drinking alcohol ethanol. Then they pressed a tiny drop of a protein solution from the point. Within short time the water contained in the protein solution changed into the alcohol. Back few Hunderstel millimeter remained a large bead of pure protein, reports the researchers in the "Biophysical journal". The procedure works so carefully that in glass transferred enzymes are again functional after renewed addition of water, resulted in first tests with four different proteins. The reason for the fact might be that only the water molecules change into the environment of the proteins into the alcohol. Those water molecules, which are embedded into the structure of the large protein molecules, remain against it at their place. For microbes this "structural water" is not accessible, so that the protein glass does not represent fertile soil for bacteria or mushrooms, describes Needhams colleague David Gaul. Besides protein glass is easier to manufacture and more simply manageable than freezingdried protein and can, approximately in case of therapeutic proteins, directly into the body be injected. The researchers already requested a patent on their technology. Research: Deborah L. Rickard, P. Brent Duncan, David Gaul and David Needham, department OF Mechanical engineering and of material Science, Duke University, Durham, North Carolina Publication Biophysical journal, VOL. 98 (6), pp 1075-84, DOI 10.1016/j.bpj.2009.11.043 Best greetings Jens Rabis Germany-Berlin Message #32497 From: Date: Sun, 21 Mar 2010 12:40:30 EDT Subject: Translation of German glassy protein paper Content-Language: en Hello all: Here is an on-line translation of the paper pasted here in German. The translation is pretty good in spots and otherwise it's amusing. It gives a good idea of the current state of translation programs (and would probably do much better on non-technical material.) The original text is below so those who read German better than I can make comparisons. __________________________ An elegant method for preserving EiweiBen have American Researchers developed. By tiny drops of a protein solution into a liquid super desiccant type transform the droplet into beads Protein glass. "This glass is not crystalline protein," explains David Needham of the Duke University, "it is rather a frozen liquid." Unlike in a crystal, the molecules are in a jar is not in the ranks arranged. Apparently, the dehydration successes so quickly that the relatively coarse Proteinmolekule no longer in a crystal lattice could slip. In their experiments, Needham and colleagues appeared a thin Pipette tip in decanol, a long-chain relatives of drinking alcohol Ethanol. Then they printed out a tiny drop of protein solution the top. Within a short time that went into the protein solution contained About water in the alcohol. Back stayed a few hundredths of a millimeter rough pearl pure protein, the researchers report in the "Biophysical Journal. The process works so carefully that in glass uberfuhrte enzymes after further addition of water are again funktionstuchtig, initial tests showed with four different proteins. The reason for this could be that only the Water molecules in the vicinity of the proteins ubergehen in alcohol. Those Water molecules that are embedded in the structure of the coarse Proteinmolekule are, however, remain in place. For microbes is this "structural water" is not accessible, so that the Protein not Glass Nahrboden for bacteria or fungi constitutes explained Needham colleague David Gaul. In addition, protein glass is easier to produce and easier to use as a freeze-dried protein and konne, such as The case of therapeutic EiweiBe be injected directly into the body. A Patent on their technique, the researchers have applied already. Research: Deborah L. Rickard, P. Brent Duncan, David and David Gaul Needham, Department of Mechanical Engineering and Materials Science, Duke University, Durham, North Carolina Publication from Biophysical Journal, Vol 98 (6), pp 1075-84, DOI 10.1016/j.bpj.2009.11.043 "End of quote, source: In a message dated 3/21/2010 3:00:25 A.M. Mountain Daylight Time, writes: Message #32495 From: "Jens Rabis" <> References: <> Subject: AW: CryoNet #32492 - #32494 Date: Sat, 20 Mar 2010 18:02:00 +0100 Betreff: Message #32494 Date: Fri, 19 Mar 2010 19:53:11 -0800 (PST) From: Subject: New Technique Turns Proteins Into Glass **************************** Information in German: Zitat: " Protein zu Glasperlen 19. Marz 2010 12:17 Eine elegante Methode zur Konservierung von EiweiBen haben amerikanische Forscher entwickelt. Indem sie winzige Tropfen einer Proteinlosung in ein flussiges Trockenmittel geben, verwandeln sich die Tropfchen in Perlen aus Proteinglas. "Dieses Proteinglas ist nicht kristallin", erklart David Needham von der Duke University, "es ist vielmehr eine erstarrte Flussigkeit." Anders als in einem Kristall, seien die Molekule in einem Glas nicht in Reih und Glied angeordnet. Offenbar erfolge der Wasserentzug so rasch, dass die vergleichsweise groBen Proteinmolekule nicht mehr in ein Kristallgitter rutschen konnten. Bei ihren Experimenten tauchten Needham und Kollegen eine dunne Pipettenspitze in Dekanol, einen langkettigen Verwandten des Trinkalkohols Ethanol. Dann druckten sie einen winzigen Tropfen einer Proteinlosung aus der Spitze. Binnen kurzer Zeit ging das in der Proteinlosung enthaltene Wasser in den Alkohol uber. Zuruck blieb eine wenige Hunderstel Millimeter groBe Perle reinen Proteins, berichten die Forscher im "Biophysical Journal". Das Verfahren arbeitet so schonend, dass in Glas uberfuhrte Enzyme nach erneuter Zugabe von Wasser wieder funktionstuchtig sind, ergaben erste Tests mit vier verschiedenen Proteinen. Der Grund dafur durfte sein, dass nur die Wassermolekule in der Umgebung der Proteine in den Alkohol ubergehen. Jene Wassermolekule, die in die Struktur der groBen Proteinmolekule eingebettet sind, bleiben dagegen an ihrem Platz. Fur Mikroben sei dieses "Strukturwasser" nicht zuganglich, sodass das Proteinglas keinen Nahrboden fur Bakterien oder Pilze darstelle, erlautert Needhams Kollege David Gaul. Zudem sei Proteinglas leichter herzustellen und einfacher handhabbar als gefriergetrocknetes Protein und konne, etwa im Falle therapeutischer EiweiBe, direkt in den Korper injiziert werden. Ein Patent auf ihre Technik haben die Forscher bereits beantragt. Forschung: Deborah L. Rickard, P. Brent Duncan, David Gaul und David Needham, Department of Mechanical Engineering and Materials Science, Duke University, Durham, North Carolina Veroffentlichung Biophysical Journal, Vol. 98(6), pp 1075-84, DOI 10.1016/j.bpj.2009.11.043" Zitat Ende, Quelle: http://www.scienceticker.info/2010/03/19/protein-zu-glasperlen/ Best greetings Jens Rabis Germany-Berlin Content-Type: text/html; charset="UTF-8" [ AUTOMATICALLY SKIPPING HTML ENCODING! ] Rate This Message: http://www.cryonet.org/cgi-bin/rate.cgi?msg=32497 Rate This Message: http://www.cryonet.org/cgi-bin/rate.cgi?msg=32501