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Recent News and Articles on the Keywords: protein + inside + 0.29  Related to the article below (Last Update: 8/5/2008)

Chill out with cool pops
The State, SC - Jul 29, 2008
Icy Treats for Everyone? (Quirk Books, $15.95) Calories, 49.38; protein, 1.07 grams; carbohydrates, 11.97 grams; total fat, 0.29 grams; cholesterol, ...
Online extra: Summer slaws
Grand Forks Herald, ND - Jul 22, 2008
Approximate nutritional analysis per serving with plain low-fat yogurt: 203 calories, 18 percent calories from fat, 4 grams total fat, 0.29 gram saturated ...
Effect of Simvastatin on Cognitive Functioning in Children With ...
Journal of American Medical Association (subscription), IL - Jul 15, 2008
Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity. Proc Natl Acad Sci US A. 1992 ...
Tyson Reports Third Quarter and Nine Months Results
CNNMoney.com (press release) - Jul 28, 2008
The company produces a wide variety of protein-based and prepared food products and is the recognized market leader in the retail and foodservice markets it ...TSN
Specific Lipids Supply Critical Negative Spontaneous Curvature-An ...
RedOrbit, TX - Jul 25, 2008
After CHOL depletion using a standardized treatment with 2 mM mbetaed (25,29), the specific curvature contributed by CHOL was -1.51 +- 0.29 amol ...
Source: Google News

… of Water on Protein Structure. An Analysis of the Preferences of Amino Acid Residues for the Inside … -
DH Wertz, HA Scheraga - Macromolecules, 1978 - pubs.acs.org
... structures are generally buried inside the protein and thus ... of Conformational
Interconversion in Going from the Inside ... 0.17 0.37 0.03 0.61 0.67 0.29 0.20 0.16 ...

… vesicle phospholipids catalyzed by the phosphatidylcholine exchange protein. Measurement of inside- … -
JE Rothman, EA Dawidowicz - Biochemistry, 1975 - pubs.acs.org
... of Inside-Outside Transitions ... Protein was measured by the method of Lowry et al ... the
known (Rouser et al., 1968) mole fraction of phospholipid which is PC, 0.29. ...

Cystic Fibrosis Transmembrane Conductance Regulator Inverts Protein Kinase A-mediated Regulation of … -
MJ Stutts, BC Rossier, RC Boucher - Journal of Biological Chemistry, 1997 - ASBMB
... the effects of cAMP-dependent protein-phosphorylating conditions ... 28) without CFTR
and 2.29 ? 0.29 (n = 26 ... Excised inside out patches or cell-attached patches ...

… Model Recognition Approach to the Prediction of All-Helical Membrane Protein Structure and Topology -
DT Jones, WR Taylor, JM Thornton - Biochemistry, 1994 - pubs.acs.org
... The most significant components of the Page 4. Membrane Protein Topology Prediction
Loop inside Biochemistry, Vol. 33, No. 10, 1994 3041 Loop outside ...

Refinement of protein structures in explicit solvent -
JP Linge, MA Williams, CAEM Spronk, AMJJ Bonvin, M … - Proteins Structure Function and Genetics, 2003 - doi.wiley.com
... chain planarity (PLNCHK), improper dihedral angles (HNDCHK), and the inside/outside
distribution ... consider the bond lengths b ij in a given protein, where each ...

Protein and DNA contents in sperm from an infertile human male possessing protamine defects that … -
G Bench, MH Corzett, L De Yebra, R Oliva, R … - Molecular Reproduction and Development, 1998 - doi.wiley.com
... Because the protamines which constitute the majority of the protein inside human
sperm nuclei contain a known number of ... Protamine 2a/total protamine 0.29 0.02 ...

A Molecular Dynamics Study of the Pores Formed by Escherichia coli OmpF Porin in a Fully Hydrated … -
DP Tieleman, HJC Berendsen - Biophysical Journal, 1998 - Biophysical Soc
... nm, and maximum radii of 0.33 nm and 0.29 nm ... the short loops on the intracellular
side of the protein. ... become narrower and the dipole magnitudes inside the pore ...

… the Synthesis of 3-Oxygenated Ingenanes. The First Ingenol Analogs with High Affinity for Protein …
JD Winkler, BC Hong, A Bahador, MG Kazanietz, PM … - The Journal of Organic Chemistry, 1995 - pubs.acs.org
... the structural requirements for the activation of protein ... synthesis of the carbocyclic
ring system of the ingenanes that embodies an ?inside-outside? or ...

Simple model to study insertion of a protein into a membrane -
R Bonaccini, F Seno - Physical Review E, 1999 - APS
... 0.37 0.41 0.47 0.27 0.28 0.40 0.41 0.45 0.45 ? 0.11 0.22 0.29 0.37 0.38 ... so one might
also be able to determine the structure of the protein inside the membrane ...

[PDF] Patterning Enzymes Inside Microfluidic Channels via Photoattachment Chemistry -
MA Holden, SY Jung, PS Cremer - Anal. Chem, 2004 - chem.tamu.edu
... B4F was again patterned in patches inside fibrinogen-coated ... 4 streptavidin
molecules/?m, of this protein were bound ... patch was at most 0.8 mm ? 0.29 mm, this ...
-

Source: Google Scholar

The closest look ever at native human tissue

A powerful microscope technique reveals the molecular organization of skin

 

Seeing proteins in their natural environment and interactions inside cells has been a long-standing goal. Using an advanced microscopy technique called cryo-electron tomography, researchers from the European Molecular Biology Laboratory [EMBL] have visualised proteins responsible for cell-cell contacts for the first time. In this week’s issue of Nature they publish the first 3D image of human skin at molecular resolution and reveal the molecular Velcro-like organisation that interlinks cells.

“This is a real breakthrough in two respects,” says Achilleas Frangakis, group leader at EMBL. “Never before has it been possible to look in three dimensions at a tissue so close to its native state at such a high resolution. We can now see details at the scale of a few millionths of a millimetre. In this way we have gained a new view on the interactions of molecules that underlie cell adhesion in tissues – a mechanism that has been disputed over decades.”

So far, the only information available about a protein’s position and interactions in a cell was based on either light microscopy images at poor resolution or techniques that remove proteins from their natural context. Frangakis and his group have been developing a technique called cryo-electron tomography, with which a cell or tissue is instantly frozen in its natural state and then examined with an electron micro-scope. Electron microscopy normally requires tissue to be treated with chemicals or coated in metal, a procedure that disturbs the natural state of a sample. With cyro-electron tomography, images are taken of the untreated sample from different directions and assembled into an accurate 3D image by a computer.

The researchers applied this technique to observe proteins that are crucial for the integrity of tissues and organs like the skin and the heart, but also play an important role in cell proliferation. These proteins, called cadherins, are anchored in cell membranes and interact with each other to bring cells close together and interlink them tightly.

“We could see the interaction between two cadherins directly, and this revealed where the strength of human skin comes from,” says Ashraf Al-Amoudi, who carried out the work in Frangakis’ lab. “The trick is that each cadherin binds twice: once to a molecule from the juxtaposed cell, and once to its next-door neighbour. The system works a bit like specialised Velcro and establishes very tight contacts between cells.”

The new insights into the cadherin system broadens the understanding of structural aspects of cell adhesion and shed light on other crucial processes such as cell proliferation. The technical advances achieved in cryo-electron tomography of frozen sections open up new possibilities to study more systems at native conditions with molecular resolution.

Skin Cell Electron Tomogram

Caption: This 3-D reconstruction of a human skin cell was produced by electron tomography and shows organelles in different colours: regions of cell-cell contact (sandy brown), nucleus and nuclear envelope (blue) with pores (red), microtubules (green), mitochondria (purple), endoplasmic reticulum (steel blue).

Credit: Achilleas Frangakis EMBL

 

 

Cadherins Close-up

Caption: 3-D visualization of interacting cadherin molecules in their native arrangement. Known molecular structures of cadherins (grey and red ribbons) are fit into the electron tomogram (multicolour) of the complex.

Credit: Achilleas Frangakis, EMBL

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