80 research outputs found

    Structural Aspects Of Protein Synthesis

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    Labor pains in the early days of the Nobel Committee for Chemistry

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    Human activities have been marred for ages by conflicts of interest. This is no less true in the field of science. In the early years of the Nobel Prizes, little attention was focused on this aspect, but awareness steadily grew. In particular, this concerned Swedes nominated for Nobel Prizes, who were most likely themselves members of the Royal Swedish Academy of Sciences, but whose fellows at the Academy should treat them equally with respect to foreign nominees. In addition, conflicts of interest can arise when committee members have close contacts with nominated scientists, regardless of nationality

    Biochemistry. Getting Close to Termination

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    Foreword

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    An enzyme in disguise

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    Deepening ribosomal insights

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    The remarkable progress of cryoelectron microscopy and crystallography in elucidating ribosomal structure and function continues. Most recently, two papers about complete 70S ribosomes from Thermus thermophilus at 2.8- and 3.7-angstrom resolution give us more details about the conformations of bound transfer RNA (tRNA) molecules; the bridges between subunits; the locations and roles of proteins, magnesium ions, and water molecules; and the dynamics of ribosomes. Very significant new insights have been gained, particularly for the tRNAs, which can only be studied in their entirety in full ribosomes

    Crystallography of the past and in the future

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    This paper is partly a summary of the book ‘From a grain of salt to the ribosome’ [1], with extension on some points. Sometimes the developments in science may be very rapid and not fully appreciated at all corners of the scientific society. Harry Clary Jones was a well-known chemist at Johns Hopkins University at the turn of the previous century. He had, in his earlier days, spent time in the laboratories of Wilhelm Ostwald in Leipzig, Svante Arrhenius in Stockholm and Jacobus van’t Hoff in Amsterdam. He wrote many papers and twelve books. In 1913 he claimed in a book [2]: We do not know the formula of rock salt, or of ice; and we have no reliable means of finding out these simplest matters about solids. Our ignorance of solids is very nearly complete. It is evident that he was unaware of the very recent developments and the revolution in chemistry that had just taken place with the birth of X-ray crystallography

    On the complementarity of methods in structural biology

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    Structural biology has transformed a number of fields of biochemistry and biology. A few examples are the following. The allosteric uptake and release of oxygen from haemoglobin obtained an elegant description from the work of Perutz [ Perutz ( 1970), Nature ( London), 227, 726 - 739; Perutz et al. ( 1998), Annu. Rev. Biophys. Biomol. Struct. 27, 1 - 34]. The structure of tRNA highlighted the fact that the two functional facets of the molecule, the anticodon and the 30- end, which is charged with amino acids, were 75 A apart [ Robertus et al. ( 1974), Nature ( London), 250, 546 - 551; Kim et al. ( 1974), Science, 185, 435 - 440]. This had interesting consequences both for charging by tRNA synthetases and for the role of tRNA as the adaptor in protein synthesis on the ribosome. The structure of the ATP synthase illustrated how the enzyme could hydrolyze or synthesize ATP by a rotating mechanism [ Abrahams et al. ( 1994), Nature ( London), 370, 621 - 628]. This transformation is a consequence of the fact that such structural insights on different levels and of different characters can provide a basis for the interpretation or reinterpretation of old observations. In addition, the design of experiments from a structural basis has become more relevant and focused
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