THERMAL STABILITY

subtilisin-cleaved F-actin. These results confirm that the DNaseI-bindingloop is involved in the stabilization of the actin structure, both in mono-mers and in the filament subunits, and suggest that the thermal stability ofactin depends, at least partially, on the conformation of the nu[r]

the queries about how the higher vertebrate DNases Iacquired their thermal stabilities described above. In thisstudy, we purified DNases I from the pancreases of threesnake species, Elaphe quadrivirgata (Shima-hebi in Japan-ese) and Elaphe climacophora (Aodaisho) of the ColubridaeOPPEL and Agk[r]

´aux, unpublished data).Fig. 3. Temperature dependence of the amide I¢ region of FU HpH-dof b-HpH. (A) Non-deconvoluted spectra are shown every 5 °Cinthe range 25–90 °C. The arrows indicate the direction of the spec-tral changes with temperature. (B) Fourier-deconvoluted IR spec-trum of FU HpH-d in[r]

sive representation of the correlation between themutations is shown in Fig. 1 (redrawn from the datain Table 1). Interestingly, mutants AS1–AS3, showingDirected evolution of tyrosine phenol-lyase E. Rha et al.6188 FEBS Journal 276 (2009) 6187–6194 ª 2009 The Authors Journal compilation ª 2009 FEBSn[r]

tural differences. Several minor modifications appeared to beresponsible for the increased thermal stability of family 11xylanases: (a) higher Thr : Ser ratio (b) increased number ofcharged residues, especially Arg, resulting in enhanced polarinteractions, and (c) improved stabilization[r]

ASNase) [16] were subjected to directed evolution,with a view to find variants with improved thermosta-bility. Enhancing the stability of l-ASNase by proteinengineering improves its body-residence time, andthereby minimizes immunosuppressive effects by lower-ing the therapeutic dose. After one[r]

Department of Chemical Enzymology,Faculty of Chemistry, Moscow State University, Moscow, RussiaThe thermal stability of peroxidase from leaves of the Africanoil palm tree Elaeis guineensis (AOPTP) at pH 3.0 wasstudied by differential scanning calorimetry (DSC), intrinsicfluorescence, CD[r]

Background: The RNA-dependent RNA polymerase of Influenza A virus is a determinant of viralpathogenicity and host range that is responsible for transcribing and replicating the negative sensesegmented viral genome (vRNA). Transcription produces capped and polyadenylated mRNAswhereas genome replicati[r]

[5] A.A. Vasiliev, R.G. Pavelko, S.Y. Gogish-Klushin, D.Y. Kharitonov, O.S. Gogish-Klushina, A.V. Sokolov, A.V. Pisliakov, N.N. Samotaev, Alumina MEMS platformfor impulse semiconductor and IR optic gas sensors, Sens. Actuat. B: Chem. 132(1) (2008) 216–223.[6] L. Wang, X.Y. Qin, W. Xiong, L. Chen, M.[r]

D83G, which results in a 33.06% decrease in DH com-pared to wild-type SNase, is also located between thetwo subdomains. These results imply that E75, D77and D83 are part of the same local stable area. Fromthis study, E129G and E101G mutations resulted indecreases of 44.13% and 28.17%, respectively,[r]

protein for their studies. We cannot confirm difficulties inproducing recombinant HIV gp41, and a very satisfactoryyield of 60 mg of pure protein per litre of bacterial culturewas reproducibly obtained. Peisajovich et al.[38]haveextrapolated their data obtained with SIV gp41 to HIVgp41. The authors ra[r]

(CD) to investigate thermal unfolding of recombinant fibroblast isoformsof a-tropomyosin (Tm) in comparison with that of smooth muscle Tm.These two nonmuscle Tm isoforms 5a and 5b differ internally only byexons 6b ⁄ 6a, and they both differ from smooth muscle Tm by theN-terminal exon 1b which[r]

changes in the chromatographic behaviour.DiscussionThe near-UV CD spectrum of PSP-I ⁄ PSP-II reflectsthe specific environment of chiral aromatic side chainsin the tertiary structure of the folded protein, and theband intensities decrease in a sigmoidal way as ther-mal denaturation occurs. In particula[r]

investigated by applying an immunoprecipitation protocolafter metabolic labelling of the wild-type and mutant a1subunits. The immunoprecipitation method was preferredover a standard Western blot to prevent possible degrada-tion of the mutant a1 subunits, which are known to be atarget for proteases u[r]

up to ®ve and seven times higher, respectively, for all themutants, than for the wild-type XI.Inhibition by xylitol. The extended a cyclic forms of thesubstrates xylose and glucose have binding closely resem-bling that observed for the acyclic polyol inhibitor xylitol[34,35]. Competitive i nhibition[r]

temperature has an effect on the amounts of tetramericY42H protein formed, however, they could not distinguishbetween a defect in folding/tetramer assembly and decreasedstability of the assembled tetrameric mutant pro tein.To address this question we used the purified recombin-ant MCAD variant protei[r]

Polypropylene/ maleic anhydride /organic montmorillonite nanocomposites (PP/ MA/ Org-MMT) have been prepared via direct melt intercalation in an internal mixer. Maleic anhydride (MA) was used as a compatibilizer to improve the dispersability of the clay. The structures of nanocomposites have been ch[r]

gas sensors based on WO3has good thermal stability,sensitivity and response characteristics to ethanol gases.AcknowledgementsThis work was supported by the Natural ScienceFoundation of Yunnan Province, China.References[1] Chung YK, Kim MH, Um WS, Lee HS, Song JK, ChoiSC, Yi KM, Lee MJ,[r]

pure EPDM when 10% weight loss was selected as apoint of comparison. This is due to the exfoliated LDHnanolayer, which in turn, obstructs the internal diffu-sion of heat and gaseous small molecules formedduring thermal oxidation [18, 19]. For higher LDHloading, the thermal stability[r]

NÔI DUNG CỦA PHẦN 1 BAO GỒM: • Definitions of Stability. • Types of Stability. • Angular Stability Analysis. • Operational Limits of Synchronous Operational Limits of Synchronous Machines.