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hutingting银虫 (正式写手)
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[求助]
求一篇英文文章的收录号
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| 求助一篇英文文章的收录号？ 谢谢！Tingting Hu, Shi-Zhong Luo*. Phosphorylation-Induced Structural Changes in the C-Terminus of c-Fos Detected by CD and NMR. International Journal of Peptide Research and Therapeutics. 2011, 17(1): 19-30. |
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lxj341401
至尊木虫 (著名写手)
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【答案】应助回帖
★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★
感谢参与，应助指数 +1
小丹木木: 金币+3, 鼓励应助 2012-05-22 15:12:46
hutingting: 金币+10, ★★★★★最佳答案, 谢谢 2012-05-22 20:48:05
感谢参与，应助指数 +1
小丹木木: 金币+3, 鼓励应助 2012-05-22 15:12:46
hutingting: 金币+10, ★★★★★最佳答案, 谢谢 2012-05-22 20:48:05
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WOS:000288710700003 FN Thomson Reuters Web of Knowledge VR 1.0 PT J AU Hu, TT Luo, SZ AF Hu, Ting-Ting Luo, Shi-Zhong TI Phosphorylation-Induced Structural Changes in the C-Terminus of c-Fos Detected by CD and NMR SO INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS LA English DT Article DE c-Fos; NMR spectroscopy; CD spectroscopy; Ser phosphorylation; Hydrogen bonds; Turn structure ID DEPENDENT PROTEIN-KINASE; DNA-BINDING DOMAINS; TRANSCRIPTION FACTOR; TRANSFORMING ACTIVITY; ACTIVATION DOMAIN; JUN; CONFORMATION; PHOSPHOPEPTIDES; EXPRESSION; PEPTIDES AB The major modification of the c-Fos protein involves serine phosphoesterification at the sites located at the extreme C-terminus. Several transcriptionally important protein-protein interactions involving c-Fos are mediated by the C-terminus domain phosphorylation. A series of peptides and phosphopeptides corresponding to C-terminus (359-380) of c-Fos protein were synthesized and their conformations were determined by CD spectroscopy and (1)H-NMR spectroscopy. The nonphosphorylated peptide (Fos-C) adopts an essentially random-coil conformation in aqueous solution as shown by CD spectroscopy, but becomes slightly more ordered into a type I turn by adding up to 80% trifluoroethanol (TFE) to increase the solvent hydrophobicity. There is tentative NMR evidence for a small population of species containing a type I turn at residues SPTL in the Fos-C. Phosphorylation at S(362) induces local conformational changes that can be attributed to the formation of local hydrogen bonds between the phosphate group and nearby amide protons, including additional medium-range (epsilon-H(N) of R(359)) effects. Upon phosphorylation at S(374), a hydrogen bond between the amide proton and phosphate group of pS(374) is formed. However, the most significant changes upon phosphorylation at S(374) are the destabilization of this turn structure, which is strongly supported by CD and NMR spectroscopy. C1 [Hu, Ting-Ting; Luo, Shi-Zhong] Beijing Univ Chem Technol, Beijing Key Lab Bioproc, Coll Life Sci & Technol, Beijing 100029, Peoples R China. [Luo, Shi-Zhong] Tsinghua Univ, Dept Chem, Key Lab Bioorgan Phosphorus Chem & Chem Biol, Minist Educ, Beijing 100084, Peoples R China. RP Luo, SZ (reprint author), Beijing Univ Chem Technol, Beijing Key Lab Bioproc, Coll Life Sci & Technol, Beijing 100029, Peoples R China EM luosz@mail.buct.edu.cn FU National Natural Science Foundation of China[21002007]; Specialized Research Fund for the Doctoral Program of Higher Education, and genetically modified organisms breeding major projects[2009ZX08012-001B] FX We thank Dr. Hiroshi Nakanishi and Dr. Xu-Rong Qin for technical supporting and help discussions. The project sponsored by the National Natural Science Foundation of China (No. 21002007), Specialized Research Fund for the Doctoral Program of Higher Education, and genetically modified organisms breeding major projects (No. 2009ZX08012-001B). NR 38 TC 0 Z9 0 PU SPRINGER PI NEW YORK PA 233 SPRING ST, NEW YORK, NY 10013 USA SN 1573-3149 J9 INT J PEPT RES THER JI Int. J. Pept. Res. Ther. PD MAR PY 2011 VL 17 IS 1 BP 19 EP 30 DI 10.1007/s10989-010-9236-6 PG 12 WC Biochemistry & Molecular Biology SC Biochemistry & Molecular Biology GA 739IT UT WOS:000288710700003 |
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