Top 7 in biochemistry

linkurl:1. Breakthrough in nano-imaging;http://f1000.com/8325958?key=9r78ddts24dp3f7Powerful, ultra-short X-ray laser pulses may allow researchers to image the structures of a wide range of membrane protein complexes. In contrast to traditional x-ray crystallography, which requires large protein crystals, the new technique can visualize nano-sized crystals with limited radiation damage by combining thousands of diffraction patterns to create 3D structures at sub-nanometer resolution.H.N. Chapman et al., "Femtosecond X-ray protein nanocrystallography,"linkurl: Nature,;http://www.nature.com/nature/journal/v470/n7332/full/nature09750.html 470:73-7, 2011. Evaluated by Thomas Meier, Max Planck Inst Biophysics, Germany; Andrey Kovalevsky and Paul Langan, Los Alamos National Lab; Yuval Mazor and Nathan Nelson, Tel Aviv Univ, Israel; Tetsuji Okada, Gakushuin Univ, Japan; Laurie Betts and Matt Redinbo, Univ North Carolina at Chapel Hill. linkurl:Free F1000 Evaluation;http://f1000.com/8325958?key=9r78ddts24dp3f7 linkurl:2. Identifying the unknown;http://f1000.com/7792962?key=dx0nw38p878tf3l

Image: flickr, AJC1

Researchers present a novel method for identifying antibody biomarkers for diseases without known antigens. The technique, which involves searching for antibodies that bind to various synthetic molecules, may prove useful for identifying diagnostic markers in a wide variety of diseases.M.M. Reddy, et al., "Identification of candidate IgG biomarkers for Alzheimer's disease via combinatorial library screening," linkurl:Cell,;http://www.ncbi.nlm.nih.gov/sites/entrez/21215375?dopt=Abstract&holding=f1000%2Cf1000m 144:132-42, 2011. Evaluated by Angela Vincent, Univ of Oxford, UK; Robert Powers, Univ of Nebraska; Soumitra Ghosh and Kavita Shah, Purdue Univ; Ivan Gerling, Univ Tennessee Health Sci Cen; David Holtzman, Wash Univ School of Med. linkurl:Free F1000 Evaluation;http://f1000.com/7792962?key=dx0nw38p878tf3l linkurl:3. The united states of RNA;http://f1000.com/2510956?key=t5tl21pzzyl4gmhThe active or native form of complex biomolecules is generally thought to be the single most stable form, but experiments with an RNA enzyme reveal that its "native state" is in fact an ensemble of multiple conformations -- complicating the understanding of how structure dictates the function of these enzymes. S.V. Solomatin et al., "Multiple native states reveal persistent ruggedness of an RNA folding landscape," linkurl:Nature,;http://www.nature.com/nature/journal/v463/n7281/full/nature08717.html 463:681-4, 2010. Evaluated by Douglas Turner, Univ Rochester; Daniel MacDougall, Margaret Elvekrog, and Ruben Gonzalez, Columbia Univ; Pascale Legault, Univ de Montreal, Canada; Robert Batey, Univ Colorado. linkurl:Free F1000 Evaluation;http://f1000.com/2510956?key=t5tl21pzzyl4gmh linkurl:4. Ribosome assembly up close;http://f1000.com/6901956?key=32t9h7nnvsqr6jp The self-assembly of the 30S subunit of bacterial ribosomes is observed in vitro with a novel use of electron microscopy combined with mass spectrometry -- revealing clues about how the process occurs in vivo and offering a powerful method for studying the assembly of other biological complexes. A.M. Mulder, et al., "Visualizing ribosome biogenesis: parallel assembly pathways for the 30S subunit,"linkurl:Science,;http://www.sciencemag.org/content/330/6004/673.abstract 330:673-7, 2010. Evaluations by Junjie Zhang and Michael Levitt, Stanford Univ; Pascale Legault, Univ. Montreal; Mikael Akke, Lund University, Sweden. linkurl:Free F1000 Evaluation;http://f1000.com/6901956?key=32t9h7nnvsqr6jp linkurl:5. Largest virus imaged on nano-scalecaptured;http://f1000.com/8357960?key=8pfgr6j7w9b7gh4Using the short, ultra powerful X-ray laser pulses described above, researchers obtained the structure of both the inside and outside of the largest known virus, the mimivirus, with a resolution that rivals that of electron microscopy. Because no preparations such as crystallization were required, this procedure may be used to study live cells, as well as particles that are impossible to crystallize. M.M. Seibert et al., "Single mimivirus particles intercepted and imaged with an X-ray laser," linkurl:Nature,;http://www.nature.com/nature/journal/v470/n7332/full/nature09748.html 470:78-81, 2011. Evaluated by Brian Adair and M Amin Arnaout, Harvard Med School; Andrey Kovalevsky and Paul Langan, Los Alamos National Lab; P Shing Ho, Colorado State Univ. linkurl:Free F1000 Evaluation;http://f1000.com/8357960?key=8pfgr6j7w9b7gh4 linkurl:6. Recreating virtual membranes;http://www.f1000biology.com/article/0kj5pb4nfv57049/id/8501956Nearly four years old, this paper presents a powerful and widely adopted modeling system, known as the MARTINI force field, which allows for the efficient simulation of a lipid membrane, including properties such as pore formation, the effect of cholesterol distribution, and stress across the bilayer.

S.J. Marrink et al., "The MARTINI force field: coarse grained model for biomolecular simulations," linkurl:J Phys Chem B,;http://pubs.acs.org/doi/abs/10.1021/jp071097f 111:7812-24, 2007. Evaluated Nathan Baker, Pacific Northwest National Lab. linkurl:Free F1000 Evaluation;http://www.f1000biology.com/article/0kj5pb4nfv57049/id/8501956 linkurl:7. Studying wet proteins;http://www.f1000biology.com/article/yy7tlsnfhsr60vx/id/7994956While water molecules are known to affect the structure and function of proteins, little is known about this interaction. Researchers describe a method for studying the effects of water and other solvents on proteins that involves trapping proteins inside small spherical structures made up of fatty acids, called micelles, and probing them with nuclear magnetic resonance (NMR) spectroscopy.N.V. Nucci et al., "Site-resolved measurement of water-protein interactions by solution NMR," linkurl:Nat Struct Mol Bio,;http://www.nature.com/nsmb/journal/v18/n2/full/nsmb.1955.html 18:245-9, 2011. Evaluated by Yu Chen and Gabriele Varani, Univ of Washington; Gira Bhabha and H Jane Dyson, The Scripps Research Institute. linkurl:Free F1000 Evaluation;http://www.f1000biology.com/article/yy7tlsnfhsr60vx/id/7994956 The F1000 Top 7 is a snapshot of the highest ranked articles from a 30-day period on Faculty of 1000 biochemistry, as calculated on March 10, 2010. Faculty Members evaluate and rate the most important papers in their field. To see the latest rankings, search the database, and read daily evaluations, visit linkurl:http://f1000.com.;http://f1000.com
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[21st February 2011]