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Recent News and Articles on the Keywords: breaking point + point breaking + proteins  Related to the article below (Last Update: 5/5/2008)


E/The Environmental Magazine
Resources for Eco-Awareness and Action
E/The Environmental Magazine, CT -
There are plenty in the practical, everyday workwear category, too, like the Mary Janes that look cute but take a little breaking in. ...
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Nevertheless, cancer cells are much closer to that breaking point and because they have impaired anti-oxidant abilities, a relatively modest increase in ...SNTA
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Her teeth are breaking down. A year ago Gamble found a mysterious, possibly fatal mass of tissue growing in her snout. On top of this, Marta has developed ...
Year of tears, memories
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Showing a penchant for sports from an early age, Pohle picked up soccer first, his slender frame darting across the field to the point where his coaches had ...
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SYS-CON Media, NJ - Apr 13, 2008
By Kevin Hoffman By Max Katz Microsoft & Linux: At What Point Is It Cheaper to Just Buy Novell? By David Harrison By Richard Monson-Haefel By Yakov Fain ...PINK:NVGNF
Source: Google News

Molecular mechanistic origin of the toughness of natural adhesives, fibres and composites -
BL Smith, TE Schaeffer, M Viani, JB Thompson, NA … - Nature, 1999 - palgrave-journals.com
... and do work, but before the breaking point (the 'summit ... 2.) In natural materials,
proteins provide the ... intermediate-strength bonds that break sacrificially with ...

NF-?B and bone: The breaking point -
Y Abu-Amer, MM Tondravi - Nature Medicine, 1997 - nature.com
... 3 Number 11 p1189 NF-kappaB and bone: The breaking point Yousef Abu-Amer & M. Mehrdad
Tondravi. New findings suggest that NF-kappaB proteins regulate osteoclast ...
-

Breaking the WAVE complex: the point of Arabidopsis trichomes -
DB Szymanski - Current Opinion in Plant Biology, 2005 - Elsevier
... Breaking the WAVE complex: the point of Arabidopsis ... cellular functions of the actin
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Mechanical Properties of and Water Vapor Transferability Through Whey Protein Films -
R Mahmoud, PA Savello - Journal of Dairy Science, 1992 - Am Dairy Sci Assoc
... cerides at the isoelectric point of casein was characterized by water ... The force required
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Stretching DNA with a Receding Meniscus: Experiments and Models -
D Bensimon, AJ Simon, V Croquette, A Bensimon - Physical Review Letters, 1995 - APS
... 2(b)]. At the breaking point, we can measure the stretched and ... known to be induced
by Rec-A proteins binding to ... ie, the force [18] Fb necessary to break it: Fb ...

RELATIONSHIPS BETWEEN BINDING QUALITY OF MEAT AND MYOFIBRILLAR PROTEINS: III: Contribution of Myosin …
T NAKAYAMA, Y SATO - Journal of Texture Studies, 1971 - Blackwell Synergy
... considered to be an index of the binding quality, the higher the protein concen-
tration ... of the myosin B gel, and that the strain at the breaking point of the ...

Myosin V motor proteins Abbreviation used in this paper: PSF, point spread function. marching … -
RD Vale - The Journal of Cell Biology, 2003 - Rockefeller Univ Press
... from the joining coiled coil (the mid-point of the dimer ... Breaking down the 37-nm
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Microtubule bending and breaking in living fibroblast cells -
DJ Odde - Journal of Cell Science, 1999 - jcs.biologists.org
... straight microtubules were also observed to break on occasion ... can freely rotate about
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… in fluorescence microscopy at low light intensities by using reversibly photoswitchable proteins -
M Hofmann, C Eggeling, S Jakobs, SW Hell - Proceedings of the National Academy of Sciences, 2005 - National Acad Sciences
... APPLIED PHYSICAL SCIENCES Breaking the diffraction barrier in ... the photokinetics of
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Break-points on a progressive ratio schedule reinforced by intravenous cocaine increase following … -
EA Loh, DCS Roberts - Psychopharmacology, 1990 - Springer
... the MFB or the amygdala significantly in- crease the breaking points on a ... Even in
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Source: Google Scholar

Proteins' 'Breaking Point' Found, UK

Scientists from Oxford University have discovered the watery secrets of what makes proteins unstable.

Their fundamental research into the 'critical condition' at which the biological function of proteins is destroyed could have a profound impact on many areas of science - including biology, materials science and medicine: In particular it could give fresh insights into diseases caused by proteins misfolding and how to mimic the properties of tissues such as cartilage and collagen.

The discovery comes from quantum mechanics simulations developed by Dr David Porter and Professor Fritz Vollrath of Oxford's Department of Zoology. 'The interaction of water with proteins is central to all biology, and the point at which water-protein interactions become unstable is arguably nature's most important 'critical condition',' said Dr David Porter. 'We can use these simulations to examine the physics and chemistry of hydrogen bonding between water and amide groups in a specific protein. The predictions from our models can then be translated into real biological stress conditions - of temperature, mechanical load and chemistry - that will cause this protein to become unstable and stop functioning.'
The new research also sheds light on how the amount of water in a protein tissue affects its relative 'softness' and overall structural properties. Proteins with relatively little water will be stiff but tough - like a hard plastic - whereas a larger fraction of water (above 30 per cent) makes tissues such as elastin highly flexible and strong.

Dr Porter and Professor Vollrath originally created the simulations to try to understand how spiders 'tease' a normally stable protein solution into a solid silk thread using a combination of stress mechanisms; temperature, mechanical load and chemistry. 'It soon became clear that our silk model could be applied to many other protein stability problems,' said Professor Fritz Vollrath. 'A key innovation is that our models can map how instability develops over a time period of anything from a few seconds to a hundred years. Understanding the role of water in biological materials will be very important as we try to create new materials with predictable properties.'

The innovative use of new ways to extract critical conditions from their quantum simulations could have many other important applications in materials science: They could be used to predict the conditions under which materials will melt or move between an ordered and a less ordered state. Professor Vollrath said: 'Clearly we can learn much more from spider silk than how to make a tough material.'

Notes:

- A report of the research, 'The role of kinetics of water and amide bonding in protein instability', is published in a forthcoming issue of the RSC journal Soft Matter, an advance copy of the article is available online here.



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