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MRC Laboratory of Molecular

On the basis of simple considerations of connected motifs, Michael Leviff and Cyrus Chothia of the MRC Laboratory of Molecular Biology derived a taxonomy of protein structures and have classified domain structures into three main groups a domains, p domains, and a/p domains. In ct structures the core is built up exclusively from a helices (see Figure 2.9) in p structures the core comprises antiparallel p sheets and are usually two P sheets packed... [Pg.31]

Arthur Lesk and Cyrus Chothia at the MRC Laboratory of Molecular Biology in Cambridge, UK, compared the family of globin strucfures with the aim of answering two general questions How can amino acid sequences that are very different form proteins that are very similar in their three-dimensional structure What is the mechanism by which proteins adapt to mutations in the course of their evolution ... [Pg.42]

Figure 3.13 The hemoglobin molecule is built up of four polypeptide chains two a chains and two (3 chains. Compare this with Figure 1.1 and note that for purposes of clarity parts of the a chains are not shown here. Each chain has a three-dimensional structure similar to that of myoglobin the globin fold. In sicklecell hemoglobin Glu 6 in the (3 chain is mutated to Val, thereby creating a hydrophobic patch on the surface of the molecule. The structure of hemoglobin was determined in 1968 to 2.8 A resolution in the laboratory of Max Perutz at the MRC Laboratory of Molecular Biology, Cambridge, UK. Figure 3.13 The hemoglobin molecule is built up of four polypeptide chains two a chains and two (3 chains. Compare this with Figure 1.1 and note that for purposes of clarity parts of the a chains are not shown here. Each chain has a three-dimensional structure similar to that of myoglobin the globin fold. In sicklecell hemoglobin Glu 6 in the (3 chain is mutated to Val, thereby creating a hydrophobic patch on the surface of the molecule. The structure of hemoglobin was determined in 1968 to 2.8 A resolution in the laboratory of Max Perutz at the MRC Laboratory of Molecular Biology, Cambridge, UK.
There is one exception to the rule that requires bulky hydrophobic residues to fill the interior of eight-stranded a/p barrels in order to form a tightly packed hydrophobic core. The coenzyme Biz-dependent enzyme methylmalonyl-coenzyme A mutase, the x-ray structure of which was determined by Phil Evans and colleagues at the MRC Laboratory of Molecular... [Pg.50]

The group of Phil Evans, MRC Laboratory of Molecular Biology, Cambridge, UK, has determined x-ray structures of bacterial PFK both in the R and the T states. These studies have confirmed the above conclusions and given insight into how an allosteric enzyme accomplishes its complex behavior. [Pg.115]

MRC Laboratory of Molecular Biology University of Cambridge Cambridge, England... [Pg.506]

MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England 2LURE, Batiment209D, 91405 Orsay, France... [Pg.12]

Senior Reporter Dr. R. C. SHEPPARD MRC Laboratory of Molecular Biology, Cambridge... [Pg.304]

Chapter 6 describes the computer methods developed by Dr. Roger Staden at the MRC Laboratory of Molecular Biology, Cambridge, for handling the sequence data produced by the rapid shotgun sequencing techniques described in Chapter 4. Since... [Pg.6]

Paul D. Boyer (b. 1918 in Provo, Utah) is Professor Emeritus of the University of California at Los Angeles (UCLA). He shared half of the Nobel Prize in Chemistry in 1997 with John Walker (b. 1941), MRC Laboratory of Molecular Biology, Cambridge, England, for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP). [The other half of the 1997 chemistry Nobel Prize went to Professor Jens C. Skou (b. 1918) of Aarhus University, Denmark, for the first discovery of an ion-transporting enzyme, Na , IC-ATPase. ]... [Pg.269]

Nigel Unwin Neurobiology Division MRC Laboratory of Molecular Biology Cambridge, United Kingdom... [Pg.357]

Electron density map of the Fi-ATPase associated with a ring of 10 c-subunits from the Fq domain of ATP synthase, a molecular machine that carries out the synthesis of ATP in eubacteria, chloroplasts, and mitochondria. [Courtesy of Andrew Leslie, MRC Laboratory of Molecular Biology, Cambridge, UK.]... [Pg.59]


See other pages where MRC Laboratory of Molecular is mentioned: [Pg.23]    [Pg.176]    [Pg.210]    [Pg.213]    [Pg.404]    [Pg.7]    [Pg.303]    [Pg.139]    [Pg.421]    [Pg.203]    [Pg.389]    [Pg.270]    [Pg.1109]    [Pg.2]   


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