Protein Refolding
Mostrando 13-24 de 208 artigos, teses e dissertações.
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13. Subclonagem e expressão do domínio catalítico da jararagina: estudo do efeito das modificações pós-traducionais na atividade hemorrágica.
Metalloproteases are Zn++-dependent peptidase enzymes, richly found in Crotalidae and Viperidae snake venoms. Most snake venom metalloproteases (svMPs) are active on extracellular matrix components and this effect is thought to result in bleeding as a consequence of the basement membrane disruption in capillaries. Jararhagin is a hemorrhagic svMP from Bothro
Publicado em: 2004
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14. Protein folding: a perspective for biology, medicine and biotechnology
At the present time, protein folding is an extremely active field of research including aspects of biology, chemistry, biochemistry, computer science and physics. The fundamental principles have practical applications in the exploitation of the advances in genome research, in the understanding of different pathologies and in the design of novel proteins with
Brazilian Journal of Medical and Biological Research. Publicado em: 2001-04
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15. Desnaturação e reenovelamento da frutalina, uma lectina ligante de D galactose / Folding and unfolding of frutalin lectin
Our current understanding of the protein folding mechanism is the result of intense study employing biophysical, biochemical and theoretical methods. "In vitro", the initial state of the protein in this puzzle is its unfolded form. In the present work we have studied the refolding, after thermal denaturation, of the glycoprotein frutalin, a member of the lec
Publicado em: 1998
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16. Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein.
We describe an approach for investigating the protein folding process, using protein fragments as inhibitory probes of the refolding protein. The refolding of Escherichia coli dihydrofolate reductase (EC 1.5.1.3), reversibly unfolded in 7 M urea, was monitored by the reappearance of enzyme activity after diluting the unfolded enzyme into low urea concentrati
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17. The substrate binding domain of DnaK facilitates slow protein refolding
We examined the effects of a fragment of the substrate binding domain of DnaK on protein refolding from chemically denatured states. The fragment DnaK384-638, containing a full-length substrate binding domain, tightly binds to the unfolded protein in solution. The effects of DnaK384-638 on the reactivation of β-galactosidase and luciferase were examined at
National Academy of Sciences.
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18. Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell
We have studied the effects of macromolecular crowding on protein folding kinetics by studying the oxidative refolding of hen lysozyme in the absence and presence of high concentrations of bovine serum albumin and Ficoll 70. The heterogeneity characteristic of the lysozyme refolding process is preserved under crowded conditions. This, together with the obse
Oxford University Press.
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19. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.
The properties of molecular chaperones in protein-assisted refolding were examined in vitro using recombinant human cytosolic chaperones hsp90, hsc70, hsp70 and hdj-1, and unfolded beta-galactosidase as the substrate. In the presence of hsp70 (hsc70), hdj-1 and either ATP or ADP, denatured beta-galactosidase refolds and forms enzymatically active tetramers.
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20. Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins
Recent advances in generating active proteins through refolding of bacterial inclusion body proteins are summarized in conjunction with a short overview on inclusion body isolation and solubilization procedures. In particular, the pros and cons of well-established robust refolding techniques such as direct dilution as well as less common ones such as diafilt
BioMed Central.
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21. Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.
The isomerization of the proline peptide bond between tyrosine-92 and proline-93 in bovine pancreatic ribonuclease A has been investigated in the unfolded protein as well as during the slow refolding process. This bond is in the cis state in the native protein. By comparison of various homologous ribonucleases we show that isomerization of proline-93 is asso
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22. Measuring the refolding of β-sheets with different turn sequences on a nanosecond time scale
Whether turns play an active or passive role in protein folding remains a controversial issue at this juncture. Here we use a photolabile cage strategy in combination with laser-flash photolysis and photoacoustic calorimetry to study the effects of different turns on the kinetics of β-hairpin refolding on a nanosecond time scale. This strategy opens up a te
National Academy of Sciences.
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23. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90
The role of the abundant stress protein Hsp90 in protecting cells against stress-induced damage is not well understood. The recent discovery that a class of ansamycin antibiotics bind specifically to Hsp90 allowed us to address this problem from a new angle. We find that mammalian Hsp90, in cooperation with Hsp70, p60, and other factors, mediates the AT
The National Academy of Sciences of the USA.
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24. Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme
The fast reaction (T̄2 ≃ 50 msec) observed previously in the refolding of thermally unfolded ribonuclease A (disulfide bonds intact) has now been studied by two properties indicative of enzyme function: binding of a competitive inhibitor (2′CMP) and hydrolysis of a substrate (CpA → C > p + A). Both the binding and catalytic reactions are fast (<2 msec