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<title>Volume 42 Issue 02</title>
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<description><![CDATA[Quarterly Reviews of Biophysics, Volume 42 Issue 02 Quarterly Reviews of Biophysics  covers the whole field of biophysics, from ion channels to DNA topology and from X-ray diffraction to NMR. The journal has gained a worldwide reputation, demonstrated by its high ranking in the ISI Science Citation Index, as a forum for general and specialised communication between biophysicists working in different areas. The majority of reviews published are invited from authors who have made significant contributions to the field, who give critical, readable and sometimes controversial accounts of recent progress and problems in their speciality. Thematic issues are occasionally published. ]]></description>
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<title>QRB volume 42 issue 2 Cover and Front matter</title>
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<description><![CDATA[Miscellaneous Quarterly Reviews of Biophysics, Volume 42 Issue 02 , pp f1-f2Abstract]]></description>
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<title>QRB volume 42 issue 2 Cover and Back matter</title>
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<description><![CDATA[Miscellaneous Quarterly Reviews of Biophysics, Volume 42 Issue 02 , pp b1-b3Abstract]]></description>
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<title>Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding</title>
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<description><![CDATA[Review ArticlesArthur L. Horwich, Wayne A. Fenton,  Quarterly Reviews of Biophysics, Volume 42 Issue 02 , pp 83-116AbstractThe chaperonin ring assembly GroEL provides kinetic assistance to protein folding in the cell by binding non-native protein in the hydrophobic central cavity of an open ring and subsequently, upon binding ATP and the co-chaperonin GroES to the same ring, releasing polypeptide into a now hydrophilic encapsulated cavity where productive folding occurs in isolation. The fate of polypeptide during binding, encapsulation, and folding in the chamber has been the subject of recent experimental studies and is reviewed and considered here. We conclude that GroEL, in general, behaves passively with respect to its substrate proteins during these steps. While binding appears to be able to rescue non-native polypeptides from kinetic traps, such rescue is most likely exerted at the level of maximizing hydrophobic contact, effecting alteration of the topology of weakly structured states. Encapsulation does not appear to involve  , and if anything, polypeptide topology is compacted during this step. Finally, chamber-mediated folding appears to resemble folding in solution, except that major kinetic complications of multimolecular association are prevented.]]></description>
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<title>The Era of RNA Awakening: Structural biology of RNA in the early years</title>
<link>http://journals.cambridge.org/action/displayAbstract?fromPage=online&#x26;aid=6066032</link>
<description><![CDATA[Review ArticlesAlexander Rich,  Quarterly Reviews of Biophysics, Volume 42 Issue 02 , pp 117-137AbstractIn the mid-1950s, RNA was a somewhat mysterious molecule with unknown three-dimensional structure and little hard evidence of biological function. Changes began with the 1956 discoveries of the RNA double helix and the phenomenon of nucleic acid hybridization. Discovery of the DNA RNA hybrid helix in 1960 opened the door to understanding biological information transfer. Single-crystal X-ray diffraction analysis made it possible to precisely define the RNA double helix, discover the novel L-shaped fold of transfer RNA (tRNA), and finally reveal the complete three-dimensional tRNA structure by 1974. By then, a functional understanding of protein synthesis had developed with an appreciation of the various roles of different RNA species. This was the era of RNA awakening.]]></description>
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