User:David Canner/Sandbox main2: Difference between revisions
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On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome|Read more...]]. | On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome|Read more...]]. | ||
<div align="right">[[Avian Influenza Neuraminidase, Tamiflu and Relenza |H1N1 Flu, Tamiflu & Neuraminidase]] were featured here earlier. See [[Proteopedia:Featured article archives|all previously featured articles...]]</div> | <div align="right">[[Avian Influenza Neuraminidase, Tamiflu and Relenza |H1N1 Flu, Tamiflu & Neuraminidase]] were featured here earlier. See [[Proteopedia:Featured article archives|all previously featured articles...]]</div> | ||
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<div>[[Image:2plc.png|thumb|center|400px|(-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE) [[1v04]]]]</div> | <div>[[Image:2plc.png|thumb|center|400px|(-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE) [[1v04]]]]</div> | ||
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