一太郎 11/10/9/8 文書
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1. 18000 8 200 200000000 30 200 00 0000 00 00 0 0 00000 250 0000 00 00 00 0000 UOUO0OU000000000000000000000000000000000 UUDIDDUUDUDDUUUDDUDDUODUUDUDUUDDUUUDUUUUDUDUU 0000 0000 D Uu D Uu Uu 0000 0000 D Uu 0000 000 000 JE es H A EJ E E L3 L3 E3 EJ 00000 DUBBI 0 0 0 L1 E El ENE EEE ERE E Ep E HESSE dez T E EE IEE LT UUUOOUDmD0O0U000U0U000000000000000 0 0 UUOUOU0O0O0U0000000000000000000000000000000 UOU0OO0O0O0000000000000000000000000000000000 6 0 07000 7 No g 2001 7777 Amount ef backup data Gls day UU U0O0U0U00000000000000 MOOO00000 UUU0OU0000000000000000000000000000000000 00000000000000000000000000000000000Vo 7 Nol No2700000000000002. 00000 UBL6eEI OOOO OOOOOOOOOOOCOOOOOOOOOOOOOOOOOGO 000000000 U bonus GOOOOOOOOOOOAMOO U U bonus II UI DU IU I I UI I I D BL6B000000000000000000000000000000000000 0001 Vol 0 2001 7 7000 UUUOOU0000000000000000000 LAST UPDATE 3 5 2001 15 55 USER NAME _a admni ster A 50 for long works 50 area for short works day am9 00 pna9 00 119 FR B 1 20 SAT B 1 21 SN B 1 22 MN B 1 23 TU B 1 24 WD B 1 25 THJ B 1 26 FR B 1 27 SAT B 1 28 SUN B 1 29 MN A 1 30 TEA 1 31 WD A 1 THJ A 2 FR A 3 SAT A 4 SNA 5 MNB 6 TLE B 7 WD B 8 THJ B 9 FR B 2 10 SAT B 2 11 SUN B 2 12 2 13 TUE 2 14 WD A 2 15 THJ A 2 16 FR A 2 17 SAT A 2 18 SUN A 2 19 MN B 2 20 TLE B 2 21 WD B 2 22 THJ B 2 23 FR B 2 24 SAT B 2 25 SUN B 2 26 MN A 2 27 2 28 WD A 3 1 THJA 3 2 3 3 SAT A 3 4 SNA 3 5 MNA 3 6 TE A 3 7 WD A 3 8 THJA NNNNNNNNN ni ght bonus_ti ne day N ppon Roche c day day nachi ne study day setti ng test day Fy i sawa Pharm c day Ajinonato Co Inc c day setti ng test day day day nachi ne study day setti ng test day Kyowa FBkko Kogyo c day N ppon Roche c day Yananouchi Pharm c day N ppon Roche c day day nachi ne study day 3GeV_si ngl e bunch day 3GeV_si ngl e bunch 3GeV si ngl e bunch day 3GeV_si ngl e bu
3. Oooo 00000000 509 0 1 801 2 2500 0000 0000 0 0 0 50 9000 OOOOOOOOOOOOOOOOOOOOOOOGO 2001777010 0000 Va No g io gt TF E z CE ACE Cf ge pe 000 36 A 1520 108 SEL LOG ist mm mm mu mm E ER ERR EN HN E ER RE 0 Sei Ti i i ar i as pl kawaka ET rm eee m mmm P e 4 0001 Vol No 20017 07000 OO 000000000000000 Il Oo LEE TEES EJE EI L1 E 07000 7 No g 2001 7 7000 UOUU0O0000000000000000 x20 20000000000 130 000 130 EJ 0000000000200000000000000000 0000 00000 T seq mmx mm 2 100x 100 200x 200 100x 100 200x 200 0000 000000 7 30 58 3 45 53 5 00 54 2 30 50 WwW Ww N 0 00000 22000 OU 00000 L3 L3 L3 L3 L3 e L3 L3 C3 E3 E3 E3 E3
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7. T5 l P A Ox 86000 0 D D 1324 000 D 8600 132 4 92 7 0 1 40 0 D 0 129 36 8401 19 x 100 92 7 14 1 4v 1 540 LE ET EI DUOUO0OO0000000000000000000000000 00000 DOUD0000000000000000U0UUUUUUD 0000000 100 mx 100 200u mx 200l DOOO200000000000000000000050 0 0 ELE ce ET TET ETE E L3 E3 E3 E3 EJ Ed Fg Tz EST E 0 0 Lr 00000 8 28 4 38 5 54 3 20 16 3 UO0OO0O0OU000000000000000000000000 0400000002 0 0 0000000000 720v0 20 02 000000 100 mx 100g ml OOO000 U x ray photon 0000000000000000 G3 E ET ES 0000 200177700 99 00000 00 3 3 2
8. 2 0 0 u my 100 200 100 200 nooo 0000 0000 0000 UDDDDD D 0 0 0 00000 0000 36 aT 36 36 Oo 2 29 235 231 2 29 415 4 12 4 16 4 18 E 5 56 5 56 555 3 57 00000 59000 11 47 9 13 14 22 10 38 13 08 10 35 15 41 11 59 14 22 11 53 17 00 13 17 16 40 14 10 19 15 15 34 22 06 17 08 27 18 19 49 Oo 23 45 18 45 28 58 225 000005000 29 39 22 10 37 27 26 06 000000 2 2 49 2 48 2 49 2 47 4 05 4 10 4 07 4 06 0000090000 5 29 5 30 5 30 532 745 7 42 7 46 747 13 10 10 40 15 45 12 04 14 49 12 20 17 26 13 46 0000059000 20 46 15 41 25 53 18 25 22 03 17 03 27 14 19 44 000000000 23 21 18 20 28 33 21 00 Oo 25 36 20 36 30 48 23 17 D000000 000 31 01 23 33 38 48 27 29 32 40 25 15 40 28 29 13 00000 34 00 28 36 48 56 33 47 0000 eR 1 18 1 18 1 18 1 18 1 55 1 55 1 55 1 55 Oo 527 237 8 01 4 13 000000 000 1 42 142 142 554 3 20 828 438 000000 6o 730 345 00000 000 20 120 120 1 20 0000 Vol 7 No J 2001 7 7000
9. J apan Graduate School of Pharmaceutical Sciences Osaka University Yamadaoka Suita Osaka J apan Summary To minutely understand the effect of foreign N terminal residues on the conformational stability of human lysozyme five mutant proteins were constructed two had Met or Ala in place of the N terminal Lys residue K1M and K1A respectively and others had one additional residue Met Gly or Pro to the N terminal Lys residue Met 1 Gly 1 and Pro 1 respectively The thermodynamic parameters for denaturation of these mutant proteins were examined by differential scanning calorimetry and were compared with that of the wildtype protein Three mutants with the extra residue were significantly destabilized the changes in unfolding Gibbs energy A A G were 9 1 to 12 2 k J mol However the stability of two single substitutions at the N terminal slightly decreased the A AG values were only 0 5 to 2 5 kJ mol The results indicate that human lysozyme is destabilized by an expanded N terminal residue The crystal structural analyses of K1M K 1A and Gly 1 revealed that the introduction of a residue at the N terminal of human lysozyme caused the destruction of hydrogen bond networks with ordered water molecules resulting in the destabilization of the protein KEKO PF Enhancement in the perfection of orthorhombic
10. lysozyme crystals grown a high magnetic field 10 T Acta Cryst D56 1079 1083 2000 Takao Sato Yusuke Yamada Shinya Saijo Tetsuya Hori Raita Hirose Nobuo Tanaka Gen Sazaki Kazuo Nakajima Noriyuki Igarashi Masahiko Tanaka and Yoshiki Matsuura Department of Life Scene Graduate School of Bioscence and Biotechnology Tokyo Institute of Technology 4259 Nagatsuta Midoriku Yokohama 226 8501 J Institute for Mater amp Research Tohoku University 2 1 1 Katahira Aoba ku Senda J 980 8577 CREST J apan Science and Technology Corporation 2 1 6 Sengen Tsukuba 305 0047 J apan Institute of Materials Structure Science High Energy Accelerator Research 5 Organization 101 Oho Tsukuba 305 0801 J apan Institute for Protein Research Osaka University 3 2 Yamadaoka Suita Osaka J apan 565 0871 0001 Vol No 20017707007 Summary Orthorhombic crystals of hen egg white HEW lysozyme were grown in a homogeneous and static magnetic field of 10 T All crystals grown at 10 T were oriented such that their crystallographic c axes were parallel to the magnetic field direction and showed a narrower average full width at half maximum FWHM of the rocking curve than those grown at O T Rocking width measurements were made at the BL 10A station at the Photon Factory Tsukuba J apan using a high resolution vertical type four circle diffractomet
11. presence of its substrate deoxycytidine monophosphate at room temperature using sodium citrate as precipitant The crystals are monodinic belonging to space group C2 with unit cell parameters 174 22 b 53 12 6 7 A 8 115 29 The asymmetric unit contains one homodimer with a corresponding Vm of 2 65 Da and solvent content of 54 Native diffraction data to 1 6 resolution have been collected from two crystals using synchrotron radiation Se Won Suh Seoul National University Crystallization and preliminary X ray analysis of Saccharomyces cerevisiae 1 a key intermediate in phosphorelay signal transduction Acta Cryst D55 1219 1221 1999 M yong Cyong L ee J ae Young Lee Hyun Kyu Song and Se Won Suh Department of Chemistry College of Natural Sciences Seoul National University Seoul 151 742 South Korea Summary 1 a 167 residue protein from Saccharomyces cerevisiae plays a key role in osmosensing phosphorelay signal transduction It forms part of multistep phosphorelay system which also includes 51 1 hybrid histidine kinase and two response regulators Ssk1p and Skn7p It has been overexpressed in soluble form in Escherichia coli with a His tag at its C terminus The recombinant protein has been crystallized at room temperature using ammonium sulfate and lithium sulfate as precipitants Native diffraction data have been collected to 2 3 using synchrotron radiation The crystals are tr
12. 0 mg l broth but four extra residues Glu Ala Glu Ala were added at the N terminus of the expressed protein EAE A lysozyme To determine the effect of the four extra residues on the stability structures and folding of the protein calorimetry X ray crystal analysis and GuHCl denaturation experiments were performed The calorimetric studies showed that the EAEA lysozyme was destabilized by 9 6 kJ mol at pH 2 7 compared with the wild type protein mainly caused by the substantial decrease in the enthalpy change A On the basis of structural information on the EAEA lysozyme thermodynamic analyses show that 1 the addition of the four residues slightly affected the conformation in other parts far from the N terminus 2 the large decrease 0001 Vol No 20017 07000 in the enthalpy change due to the conformational changes would be almost compensated by the decrease in the entropy change and 3 the decrease in the Gibbs energy change between the EAEA and wild type human lysozymes could be explained by the summation of each Gibbs energy change contributing to the stabilizing factors concerning the extra residues 00000 DUDDUUDLUUIIDDUDDDUDDuDuuuu Effect of foreign N terminal residues on the conformational stability of human lysozyme Eur J Biochem 266 675 682 1999 Kazufumi Takano Kimiko Tsuchimori Yuriko Yamagata and KatsuhideYutani Institute for Protein Research Osaka University Yamadaoka Suita Osaka
13. 0000 000000 0000000 200 0 00000000000 07000 Nd 7 No g 2001 7 TI O O 000 100 00000 000 1 145070 T 0 0 f 0 0 D uu EP 08 00 UUUDUDUDDDUDUDUDDUU 9 00 0 00 0 00 0 00 0 E ESI a EZ ES E L3 Fa E Ll rr E E EJ 00 0000
14. 000000000000000000 DODO0U00000000000000000000000000U00UU00120000 0 000000 0001 Vol No 20017 07000 000 00 Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme Protein Engineering 12 841 850 1999 J un Funahashi Kazufumi Takano Yuriko Yamagata and KatsuhideYutani Institute for Protein Research Osaka University Yamadaoka Suita Osaka 565 0871 Graduate School of Pharmaceutical Sciences Osaka University Yamadaoka Suita Osaka 565 0801 J apan Summary To elucidate correlative relationships between structural change and thermodynamic stability in proteins a series of mutant human lysozymes modified at two buried positions lle56 and 11 59 were examined Their thermodynamic parameters of denaturation and crystal structures were studied by calorimetry and X ray crystallography The mutants at positions 56 and 59 exhibited different responses to a series of amino acid substitutions The changes in stability due to substitutions showed a linear correlation with changes in hydrophobicity of substituted residues having different slopes at each
15. DUDUDUUDDDUDUUUODUDUDUDUDUDDUDOUD 0000000 5 UOUO0O0OU0000000000000000000000000000 UUDIDUUDUUDDUDUUDUDIDUDDUUUDUUUDDUDUDUU UUUDUDUUUDUDDUDUDUUDUDUUDUUUDUDDUDUDOD 0 0 EVET E L3 L3 E3 LJ es 000 EI L El Fe sea ES ea saa Cc L3 L3 D m L3 C3 E3 r3 C3 C3 CJ EE EE ES E3 E Eig o L3 EJ r3 E3 isa EJ EI 1 4 00 00 00 1 0 0 0 0 000000 00
16. e and Biotechnology KIST Daejon 305 333 Korea Summary A highly thermostable xylose isomerase from Thermus caldophilus has been expressed in Esckericha coli The purified enzyme has an optimum temperature of 363 K It has been crystallized at room temperature using ammonium sulfate as a precipitant The crystal belongs to the orthorhombic space group P2 2 2 with unit cell parameters 84 35 b 123 60 c 140 24 The presence of one molecule of tetrameric xylose isomerase in the asymmetric unit gives a crystal volume per protein mass Vm of 2 1 Da and a solvent content of 41 by volume The crystals initially showed diffraction to 1 7 A Bragg spacing with synchrotron X rays and a set of native data extending to 2 3 resolution has been collected Se Won Suh Seoul National University Crystallization and preliminary X ray crystallographic analysis of deoxycytidylate hydroxymethylase from bacteriophage T4 Acta Crystal D55 1061 1063 1999 Se Hui Sohn Hyun Kyu Song Kyeongsik Min Seung e Cho J inho Moon J ae Young Lee Hyung J un Ahn Changsoo Chang Hie joon Kim and Se Won Sub Department of Chemistry College of Natural Sciences Seoul National University Seoul 151 742 South Korea 0001 Vol No 20017 07000 Summary Deoxycytidylate hydroxymethylase from bacteriophage 4 is homodimeric enzyme in which each polypeptide chain consists of 246 aminoacid residues It has been crystallized in the
17. er Crystal perfection was evaluated using the FWHM of the rocking curve the effects of the magnetic field on the quality of the crystals were examined by comparison of the FWHM of seven crystals grown at 10 and The FWH Ms of the reflections along the a b and c axes decreased by 23 5 35 3 and 27 8 respectively and those of other general reflections decreased by 17 4 42 2 in the crystals grown at high magnetic field These results clearly showed that a magnetic field of 10 T improved the crystal perfection of the orthorhombic lysozyme crystals As a result the maximum resolution of X ray diffraction increased from 1 3 A at O T to 113 at 10 T The magnetic field also affected the dimensions of the unit cell increments being 0 2 for the a and c axes and 0 1 for the b axis respectively These facts suggest that the application of a high magnetic field during crystallization might result in remarkable enhancements in the diffraction power of protein crystals having magnetic anisotropy Se Won Suh Seoul National University A thermostable xylose isomerase from Thermus caldophilus biochemical characterization crystallization and preliminary X ray analysis Acta Crystallographica D55 294 296 1999 Changsoo Chang Hyun Kyu Song Byung Chul Park Dae Sil Lee and Se Won Suh Department of Chemlstry College of Natural Sciences Seoul Natlonal University Seoul 151 742 Korea Korea Research Institute of Bioscienc
18. iclinic belonging to the space group P1 with unit cell parameters 65 78 b 66 74 c 265 75 a 106 60 210648 y 115 53 The asymmetric unit contains four molecules of the monomeric recombinant Ypdip with a corresponding Vm of 2 75 Da anda solvent content of 55 3
19. mutation site However the stability of each mutant was found to be represented by a unique equation involving physical properties calculated from mutant structures By fitting present and previous stability data for mutant human lysozymes substituted at various positions to the equation the magnitudes of the hydrophobicity of a carbon atom and the hydrophobicity of nitrogen and neutral oxygen atoms were found to be 0 178 and 0 013 kJ mol respectively It was also found that the contribution of a hydrogen bond with a length of 3 0 to protein stability was 5 1 kJ mol and the entropy loss of newly introduction of a water molecules was 7 8 mol 00000 0000000 0000000000000 Effect of extra N terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris Protein Engineering 13 299 307 2000 Shuichiro Goda Kazufumi Takano Yuriko Yamagata Yoshio Katakura and atsuhide Yutani Institute for Protein Research Osaka University Yamadaoka Suita Osaka 565 0871 Graduate School of Pharmaceutical Sciences Osaka University Yamadaoka Suita Osaka 565 0871 5 Graduate School of Engineering Osaka University Yamadaoka Suita Osaka 565 0871 apan Summary A human lysozyme expression system by Pichia pastoris was constructed with the expression vector of pPIC9 which contains the a factor signal peptide known for high secretion efficiency P pastoris expressed the human lysozyme at about 30
20. nch day 3GeV_si ngl e bunch day 3GeV_si ngl e bunch nachi ne study day N ppon Roche c day day Ki ri n Brewery day setti FE test day c day day nachi ne study day setting test day Kyowa FBkko Kogyo c day day day c day c day day day Fuj i sawa_Pharm_c day N ppon Roche c day Ei sai Co Ltd c day setti ng test Chugai Pharm c Chugai Pharm c nachi ne stu setti ng test day setting test day nachi ne study day N ppon Roche c day setting test day setting test day nachi ne study setting test V t anabe Nobuhi sa d nachi ne study bonus ti ne N ppon Roche c nachi ne study 3G amp V si ngl e bunch 3GeV si ngl e bunch 3GeV si ngl e bunch 3GV si ngl e bunch si ngl e bunch 3G amp V si ngl e bunch nachi ne study Ki rin Brewery BER _ C nachi ne_study bonus ti Chugai Pharm c Chugai Pharm c nachi ne stu setti ng test setti ng test nachi ne study CA e Bh p ng For booking systemMV L sasaki nf o hunan nagoya u ac j p _C i ndustry _d ndustry free pn 00 am 9 00 the next day ni ght ni ght ni ght ni ght ni ght ri ght 07000 7 No g 2001 7 7000 UO0OU000000000000000000 UU 000000 0000p 000 core dump 00000 image 00000
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