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Recent News and Articles on the Keywords: dark energy + researchers probe + proteins  Related to the article below (Last Update: 5/5/2008)


Pittsburgh Post Gazette
Gift helps CMU probe cosmic mystery
Pittsburgh Post Gazette, PA - Apr 20, 2008
To test theories, researchers do computer simulations of the evolution of the universe based on certain assumptions about dark matter and energy. ...
Marshall scientists eager to use probe set for May launch
The Huntsville Times - al.com, AL - Apr 10, 2008
Gamma rays are the highest energy form of radiation. Marshall scientists, along with researchers at the University of Alabama in Huntsville, ...
Source: Google News

… protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for F?rster resonance energy … -
S Ganesan, SM Ameer-beg, TTC Ng, B Vojnovic, FS … - Proceedings of the National Academy of Sciences, 2006 - National Acad Sciences
... and Human Development, Porter Neuroscience Research Center, 35 ... in the excited state
cannot accept energy from a ... Because the use of a dark acceptor liberates a ...

Energy Metabolism in Uncoupling Protein 3 Gene Knockout Mice -
AJ Vidal-Puig, D Grujic, CY Zhang, T Hagen, O Boss … - Journal of Biological Chemistry, 2000 - ASBMB
... support a primary role for UCP3 in energy dissipation ... were maintained on a 12-h
light/dark cycle ... dismutase mimetic (47) (SC52608, Monsanto Corporate Research, St ...

Fluorescence Spectroscopy of Single Biomolecules -
S Weiss - Science, 1999 - sciencemag.org
... which shortens the fluorophore's dark triplet excited ... the total signal and the energy
transfer efficiency ... the field accessible to many interested researchers. ...

Photophysics of the carotenoids associated with the xanthophyll cycle in photosynthesis
HA Frank, A Cua, V Chynwat, A Young, D Gosztola, … - Photosynthesis Research, 1994 - Springer
... Limiting light levels or dark adaptation of the ... and the University of Connecticut
Research Foundation ... of Chemical Sciences, Office of Basic Energy Sciences, US ...

Photosynthetic thermoluminescence as a simple probe of Photosystem II electron transport
Y Inoue - Biophysical Techniques in Photosynthesis, 1996 - Springer
... Yorinao Inoue Solar Energy Research Group, The Institute of ... discuss some possible
new research areas to ... suggested by observations that dark- grown gymnosperm ...

Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific … -
O Boss, S Samec, A Paoloni-Giacobino, C Rossier, A … - FEBS Letters, 1997 - Elsevier
... individually with a 12-h light-dark cycle. ... The three mitochondrial energy-transfer-
protein signature domains ... for both basic and clinical research in metabolic ...

Acetyl-coenzyme A synthetase is a lipogenic enzyme controlled by SREBP-1 and energy status -
H Sone, H Shimano, Y Sakakura, N Inoue, M Amemiya- … - American Journal of Physiology- Endocrinology And Metabolism, 2002 - Am Physiological Soc
... has also been well known among researchers in ruminology ... cages with a 12:12-h
light-dark cycle and ... could be expressed and participate in energy metabolism in ...

A high signal-to-noise Ca 2 probe composed of a single green fluorescent protein -
J Nakai, M Ohkura, K Imoto - Nature Biotechnology, 2001 - nature.com
... of probe, which uses chemiluminescence resonance energy transfer, has ... several tens
of seconds in the dark, indicating that ... signal-to-noise Ca 2+ probe based on ...

Computational tools for protein modeling -
D Xu, Y Xu, EC Uberbacher - Curr Protein Pept Sci, 2000 - ingentaconnect.com
... with high quality, is widely used by researchers in their ... the inward-facing surface
of the probe sphere as ... 90, 50, 91], such as solvation energy, entropy, and ...

COSMOLOGY: Galaxy Maps Support Theory That the Universe Is Flying to Pieces -
C Seife - Science, 2003 - sciencemag.org
... year, the Wilkinson Mi- crowave Anisotropy Probe (WMAP) team ... billion years old, flat,
and dominated by dark energy. ... The researchers did so not by targeting the ...

Source: Google Scholar

Researchers Probe Proteins' "Dark Energy"
Researchers at the University of Pennsylvania School of Medicine are the first to observe and measure the internal motion inside proteins, or its "dark energy." This research, appearing in the current issue of Nature has revealed how the internal motion of proteins affects their function and overturns the standard view of protein structure-function relationships, suggesting why rational drug design has been so difficult.

"The situation is akin to the discussion in astrophysics in which theoreticians predict that there is dark matter, or energy, that no one has yet seen," says senior author A. Joshua Wand, PhD, Benjamin Rush Professor of Biochemistry. "Biological theoreticians have been kicking around the idea that proteins have energy represented by internal motion, but no one can see it. We figured out how to see it and have begun to quantify the so-called 'dark energy' of proteins."
Proteins are malleable in shape and internal structure, which enables them to twist and turn to bind with other proteins. "The motions that we are looking at are very small, but very fast, on the time scale of billions of movements per second," explains Wand. "Proteins just twitch and shake." The internal motion represents a type of energy called entropy.

Current models of protein structure and function used in research and drug design often do not account for their non-static nature. "The traditional model is almost a composite of all the different conformations a protein could take" says Wand.

The researchers measured a protein called calmodulin and its interactions with six other proteins when bound to a protein partner one at a time. These binding partners included proteins important in smooth muscle contraction and a variety of brain functions.

Using nuclear magnetic resonance spectroscopy, the investigators were able to look at the changes in the internal motion of calmodulin itself in each of the six different protein binding situations. They found a direct correlation between a change in calmodulin's entropy a component of its stored energy - and the total entropy change leading to the formation of the calmodulin-protein complex. Finding out the contribution from individual proteins versus the entropy, or movement, of the entire protein complex has been more difficult and has been overcome in this study. From this individual contribution they deduced that changes in the entropy of the protein are indeed important to the process of calmodulin binding its partners.

"Before these unexpected results, most researchers in our field would have predicted that entropy's contribution to protein-protein interactions would be zero or negligible," says Wand. "But now it's clearly an important component of the total energy in protein binding."

Because of this new information, the researchers suggest that the entropy component may explain why drug design fails more often than it works. Currently, drugs are designed generally based on the precise structures of their biological targets, active regions on proteins that are intended to inhibit key molecules.

However, the number of designed molecules actually binding to their targets is low for many engineered molecules. "We think that this is because the design is based on a model of a static protein, not the moving, hyper protein that is constantly changing shape," say Wand. "We need to figure out how this new information fits in and perhaps drug design could be significantly improved."

Future directions include understanding whether the principles revealed by this study are universal and impact the thousands of protein-protein interactions that underlie biology and disease. As Wand explains, "Protein-protein interactions are central to 'signalling', which is often the molecular origin of diseases. Cancer, diabetes, and asthma are three important examples. We are currently looking at the role of protein entropy in the control of critical signaling events in all three."
This work was funded by grants from the National Institute of Diabetes, Digestive and Kidney Diseases. Co-authors on the study are Kendra King Frederick, Michael S. Marlow, and Kathleen G. Valentine, all from Penn.

PENN Medicine is a $3.5 billion enterprise dedicated to the related missions of medical education, biomedical research, and excellence in patient care. PENN Medicine consists of the University of Pennsylvania School of Medicine (founded in 1765 as the nation's first medical school) and the University of Pennsylvania Health System.

Penn's School of Medicine is ranked #2 in the nation for receipt of NIH research funds; and ranked #3 in the nation in U.S. News & World Report's most recent ranking of top research-oriented medical schools. Supporting 1,400 fulltime faculty and 700 students, the School of Medicine is recognized worldwide for its superior education and training of the next generation of physician-scientists and leaders of academic medicine.

The University of Pennsylvania Health System includes three hospitals, all of which have received numerous national patient-care honors [Hospital of the University of Pennsylvania; Pennsylvania Hospital, the nation's first hospital; and Penn Presbyterian Medical Center]; a faculty practice plan; a primary-care provider network; two multispecialty satellite facilities; and home care and hospice.

University of Pennsylvania School of Medicine
3600 Market St., Ste 240
Philadelphia, PA 19104
United States
http://www.med.upenn.edu
 
 
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