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Recent News and Articles on the Keywords: probe + researchers + proteins  Related to the article below (Last Update: 8/5/2008)


BBC News
Light goes out on pioneer machine
BBC News, UK -
These machines will use X-ray lasers to probe matter on time-dependent scales, allowing researchers to see, for example, the moment bonds are broken and ...
New and Exciting in PLoS Biology and PLoS Medicine
ScienceBlogs -
Surprisingly, the mutations mapped to a gene that encodes a protein unrelated to any of the known phototransduction systems in nature. ...
Key Mechanism Of Cellular Damage In Aging And Disease Discovered
Science Daily (press release) - Jul 25, 2008
In the Cell study, researchers used a newly patented, protein-based probe to discover, and make visible, for the first time, fleeting bursts of superoxide ...
BioInform's Surfing Report: Web-Based Tools and Algorithms ...
bio1nf0rm (subscription), NY - Aug 1, 2008
Links are provided from citations to relevant biological database entries, such as UniProt proteins. Text-mining methods from the research community like ...
European researchers set sights on photoreceptor proteins
BioOptics World, OK - Jul 9, 2008
In these experiments, the scientists will again use a laser pump to activate the proteins, but here they will use a very fast pulsed x-ray probe to record ...
Probes and Tags to Study Biomolecular Function: for Proteins, RNA ...
MarketWatch - Jul 9, 2008
The only resource to systematically review current experimental methods, this handy reference enables researchers to select the best solution for their ...
Vytex(TM) Natural Rubber Latex Manufacturing Test Results Get ...
MarketWatch - Jul 24, 2008
Mark is a highly-regarded researcher in latex protein interaction who is frequently called upon by employers and agencies to evaluate workplace bioaerosols ...
ChIP-on-chip
Scientist, UK - Aug 1, 2008
In ChIP cells are fixed with formaldehyde to crosslink proteins to DNA. The DNA is then harvested, fragmented, and subjected to immunoprecipitation with an ...
Driving The Innovation Economy In Ottawa
Canada NewsWire (press release), Canada - Jul 31, 2008
Dr. Natalie Goto's research team will focus on one of the proteins important for this "middle-finding" function. This will improve the understanding of ...
Presumed dinosaur flesh may just be bacterial sludge
Scientific American - Jul 30, 2008
Kaye and other researchers first used a scanning electron microscope to probe the inner, cave-like chambers in dinosaur bone samples and noted striking ...
Source: Google News

Current developments in SELDI affinity technology -
N Tang, P Tornatore, SR Weinberger? - Mass Spectrometry Reviews, 2004 - doi.wiley.com
... the successfuluseofPVDFsubstratesisthatthestrongbinding of the proteins to the ... In
that original research, single-stranded DNAwas ... onto a MALDI-MS probe tip, and ...

A fiber optic probe for monitoring protein aggregation, nucleation and crystallization -
RR Ansari, KI Suh, TL Bray, LJ DeLucas, A … - Journal of Crystal Growth, 1996 - ingentaconnect.com
... The compact probe is also equipped with a miniaturized microscope for visualization
of macroscopic protein crystals. ... Document Type: Research article. ...

[PDF] Activity-based protein profiling in vivo using a copper (I)-catalyzed azide-alkyne [3+ 2] … -
AE Speers, GC Adam, BF Cravatt - J. Am. Chem. Soc, 2003 - scripps.edu
... binding affinity for specific proteins is also ... cycloaddition chemistry should streamline
probe synthesis by ... California Breast Cancer Research Program, Activx ...
-

A Study on the Reaction Mechanisms of Protein with BPR-Zn (II) as Spectrum Probe and Its Analytical … -
K Zhu, KA Li, SY Tong - Analytical Letters, 1996 - informaworld.com
... Some researchers suggest that the effect of protein is ... to that of surfactants4, with
protein taking the ... about the reaction of spectroscopic probe with protein ...

Development of an isotope-coded activity-based probe for the quantitative profiling of cysteine … -
PF van Swieten, R Maehr, AMCH van den Nieuwendijk, … - Bioorganic & Medicinal Chemistry Letters, 2004 - Elsevier
... with either the light or heavy ICAT probe, trypsinolysis of ... 15N) and activity-based
probes targeting other proteins.[2 and 3] Current research efforts are ...

Molecular Biology: From Genome to Proteome: Looking at a Cell's Proteins -
P Kahn - Science, 1995 - sciencemag.org
... with the advent of powerful new methods ofmass spectrometry that vastly simplify
protein analysis, even on very small samples, and enable researchers to match ...

The evolution of dip-pen nanolithography -
DS Ginger, H Zhang, CA Mirkin - Angew. Chem. Int. Ed, 2004 - doi.wiley.com
... nanolithography (DPN) is a new scanning-probe based direct ... that is accessible to
any researcher who can ... His research interests center on the physical chemistry ...

Genosensor technology and the detention of interfacial nucleic acid chemistry -
M Yang, ME McGovern, M Thompson - Analytica Chimica Acta, 1997 - Elsevier
... gene sequence is identified by a DNA probe that can ... molecular biology have been used
in research laboratories to study the effects of proteins and drugs on ...

Cloning and Characterization of the Promoter Region of Human Telomerase Reverse Transcriptase Gene -
I Horikawa, PLA Cable, C Afshari, JC Barrett - Cancer Research, 1999 - AACR
... protein (TEP1) with similarity to the Tetrahymena telomerase protein p80 8 ... 18?447
in GenBank AF015950) as a hybridization probe at Research Genetics, Inc. ...

The Use of t-Butyl Hydroperoxide as a Probe for Methionine Oxidation in Proteins -
RG Keck - Analytical Biochemistry, 1996 - Elsevier
... 0131 The Use of t-Butyl Hydroperoxide as a Probe ... Recently, other researchers have
shown ... oxidant at neutral pH for a variety of proteins including recombinant hu ...

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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