Dumbbell Domains
Mostrando 1-9 de 9 artigos, teses e dissertações.
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1. Taxa de convergência de atratores de algumas equações de reação-difusão perturbadas. / Rate of convergence of attractors de some reaction-difusion equations pertubadas
In this work we study the asymptotic nonlinear dynamical of some reaction-diffusion parabolic equations under perturbations in parameter and singular perturbations in a dumbbell domain. More precisely, we treat of the attractors from these problems, we seek understand the dependence these asymptotic set of states in relationship the parameter, investigating
Publicado em: 2010
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2. "Comportamento assintótico de problemas parabólicos em domínios tipo Dumbbell" / Assimptotic Behavior for parabolic problems in Dumbbell domains
The aim of this work is to study the asymptotic dynamics of parabolic problems in dumbbell type domains. To that end firstly, we study upper semicontinuity of attractors for parabolic problems with homogeneous Neumann boundary conditions and afterwards we study the existence of stable nonconstant equilibria for reaction-diffusion problems with nonlinear Neum
Publicado em: 2004
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3. The linker of des-Glu84-calmodulin is bent.
The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand do
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4. gp160, the envelope glycoprotein of human immunodeficiency virus type 1, is a dimer of 125-kilodalton subunits stabilized through interactions between their gp41 domains.
The molecular masses, carbohydrate contents, oligomeric status, and overall molecular structure of the env glycoproteins of human immunodeficiency virus type 1--gp120, gp160, and gp41--have been determined by quantitative electron microscopy. Using purified gp160s, a water-soluble form of env purified from a recombinant vaccinia virus expression system, we h
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5. Stabilization of the long central helix of troponin C by intrahelical salt bridges between charged amino acid side chains.
The unusual dumbbell shape of troponin C is due to the presence of a long alpha-helix of nine turns that connects the amino- and carboxyl-terminal calcium-binding domains. The center of the long helix appears to be stabilized by several salt bridges. The long helix is also bent about 16 degrees at glycine-92. Calmodulin, which lacks the central glycine, also
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6. Trimeric structure for an essential protein in L1 retrotransposition
Two proteins are encoded by the mammalian retrotransposon long interspersed nuclear element 1 (LINE-1 or L1); both are essential for retrotransposition. The function of the protein encoded by the 5′-most ORF, ORF1p, is incompletely understood, although the ORF1p from mouse L1 is known to bind single-stranded nucleic acids and function as a nucleic acid cha
National Academy of Sciences.
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7. A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle mutant gene dbf4 encodes a protein kinase and is identified as CDC5.
We have isolated a multicopy suppressor of the temperature-sensitive growth phenotype of organisms carrying mutations of DBF4, a gene that is required for the initiation of chromosomal DNA replication in Saccharomyces cerevisiae and that interacts with the CDC7 protein kinase. Nucleotide sequence analysis of the suppressor gene, provisionally named MSD2, rev
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8. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
The eukaryotic translation initiation factor 4A (eIF4A) is a member of the DEA(D/H)-box RNA helicase family, a diverse group of proteins that couples an ATPase activity to RNA binding and unwinding. Previous work has provided the structure of the amino-terminal, ATP-binding domain of eIF4A. Extending those results, we have solved the structure of the ca
The National Academy of Sciences.
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9. Subunit Oligomerization and Substrate Recognition of the Escherichia coli ClpYQ (HslUV) Protease Implicated by In Vivo Protein-Protein Interactions in the Yeast Two-Hybrid System
The Escherichia coli ClpYQ (HslUV) is an ATP-dependent protease that consists of an ATPase large subunit with homology to other Clp family ATPases and a peptidase small subunit related to the proteasomal β-subunits of eukaryotes. Six identical subunits of both ClpY and ClpQ self-assemble into an oligomeric ring, and two rings of each subunit, two ClpQ rings
American Society for Microbiology.