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




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