protein S

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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/12/10 03:21:10」(JST)

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英文文献

  • NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.
  • Cembran A1, Kim J, Gao J, Veglia G.Author information 1Department of Biochemistry, Biophysics & Molecular Biology, University of Minnesota, 6-155 Jackson Hall, MN 55455, USA. vegli001@umn.edu.AbstractProteins exist as an ensemble of conformers that are distributed on free energy landscapes resembling folding funnels. While the most stable conformers populate low energy basins, protein function is often carried out through low-populated conformational states that occupy high energy basins. Ligand binding shifts the populations of these states, changing the distribution of these conformers. Understanding how the equilibrium among the states is altered upon ligand binding, interaction with other binding partners, and/or mutations and post-translational modifications is of critical importance for explaining allosteric signaling in proteins. Here, we propose a statistical analysis of the linear trajectories of NMR chemical shifts (CONCISE, COordiNated ChemIcal Shifts bEhavior) for the interpretation of protein conformational equilibria. CONCISE enables one to quantitatively measure the population shifts associated with ligand titrations and estimate the degree of collectiveness of the protein residues' response to ligand binding, giving a concise view of the structural transitions. The combination of CONCISE with thermocalorimetric and kinetic data allows one to depict a protein's approximate conformational energy landscape. We tested this method with the catalytic subunit of cAMP-dependent protein kinase A, a ubiquitous enzyme that undergoes conformational transitions upon both nucleotide and pseudo-substrate binding. When complemented with chemical shift covariance analysis (CHESCA), this new method offers both collective response and residue-specific correlations for ligand binding to proteins.
  • Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2014 Apr 14;16(14):6508-18. doi: 10.1039/c4cp00110a. Epub 2014 Mar 7.
  • Proteins exist as an ensemble of conformers that are distributed on free energy landscapes resembling folding funnels. While the most stable conformers populate low energy basins, protein function is often carried out through low-populated conformational states that occupy high energy basins. Ligand
  • PMID 24604024
  • Fibrin-based biomaterials: Modulation of macroscopic properties through rational design at the molecular level.
  • Brown AC1, Barker TH2.Author information 1The School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA; The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA.2The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA; The Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. Electronic address: thomas.barker@bme.gatech.edu.AbstractFibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury. Because of these properties and the ease of polymerization of the material, fibrin has been widely utilized as a biomaterial for over a century. Modifying the macroscopic properties of fibrin, such as elasticity and porosity, has been somewhat elusive until recently, yet with a molecular-level rational design approach it can now be somewhat easily modified through alterations of molecular interactions key to the protein's polymerization process. This review outlines the biochemistry of fibrin and discusses methods for modification of molecular interactions and their application to fibrin based biomaterials.
  • Acta biomaterialia.Acta Biomater.2014 Apr;10(4):1502-1514. doi: 10.1016/j.actbio.2013.09.008. Epub 2013 Sep 19.
  • Fibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury
  • PMID 24056097

和文文献

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関連リンク

プロテインS, protein S 測定方法 : 抗原量:EIA法(SRL), 遊離型抗原量:ラテックス凝集比濁法(LSIM)、活性(BML) 外注会社 : SRL,LSIM(旧MCM)、BML 基準範囲 : SRL 63~135%(抗原量)
Consumer-friendly information about human genetics from the U.S. National Library of Medicine. ... Protein S deficiency is a disorder of blood clotting. People with this condition have an increased risk of developing abnormal blood ...

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★リンクテーブル★
リンク元プロテインS」「PS
拡張検索90-kDa ribosomal protein S6 kinase」「70-kDa ribosomal protein S6 kinase」「ribosomal protein S6
関連記事protein」「S

プロテインS」

  [★]

protein S, PS
プロテインC

生合成

肝臓でビタミンK依存的に生合成されるタンパクは第II因子(プロトロンビン)、第VII因子第IX因子第X因子



PS」

  [★]


90-kDa ribosomal protein S6 kinase」

  [★] 90-kDaリボソームS6キナーゼ

MAPキナーゼで活性化される細胞内シグナリング酵素
p90 ribosomal S6 kinase


70-kDa ribosomal protein S6 kinase」

  [★] 70-kDaリボソームS6キナーゼ

翻訳調節に関与するリン酸化酵素
p70 S6 kinasep70S6K


ribosomal protein S6」

  [★]

リボソームタンパク質S6


protein」

  [★] 蛋白質

WordNet   license wordnet

「any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"」

PrepTutorEJDIC   license prepejdic

「蛋白(たんばく)質」


S」

  [★]

WordNet   license wordnet

「the 19th letter of the Roman alphabet」
s

PrepTutorEJDIC   license prepejdic

「sulfurの化学記号 / {略}South[ern]」




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