Multidomain Proteins
Mostrando 1-12 de 97 artigos, teses e dissertações.
-
1. Integrated experimental biophysics and molecular dynamics simulations of biomolecules in solution - the interaction of nuclear receptors with DNA response elements and the inter-domain dynamics of Cellobiohydrolase I / Estudos por modelagem e dinâmica molecular integradas a técnicas físicas para biomoléculas em solução - interação de receptores nucleares a elementos responsivos no DNA e dinâmica inter-domínios da celobiohidrolase I
Collective motions play a fundamental role in solution biomolecule dynamics and energetics. These movements can couple very distant regions in the protein structures affection, for instance, allosteric mechanisms, the establishment of macromolecular complexes, and on the integrated function of multidomain proteins as molecullar machines. In this thesis, we p
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 26/09/2011
-
2. Fusion of the subunits α and β of succinyl-CoA synthetase as a phylogenetic marker for Pezizomycotina fungi
Gene fusions, yielding the formation of multidomain proteins, are evolutionary events that can be utilized as phylogenetic markers. Here we describe a fusion gene comprising the α and β subunits of succinyl-coA synthetase, an enzyme of the TCA cycle, in Pezizomycotina fungi. This fusion is present in all Pezizomycotina with complete genome sequences and ab
Genetics and Molecular Biology. Publicado em: 26/08/2011
-
3. Estudos de macromoleculas biologicas parcialmente desestruturadas usando espalhamento de raios-X / Study of partially unstructured macromolecules using X-ray scattering
As técnicas de caracterização estrutural de macromoléculas tradicionais se baseiam no fato de uma macromolécula possuir uma conformação compacta e estruturada. Partes flexíveis ou regiões desordenadas têm sido sempre consideradas como grandes obstáculos para técnicas como a cristalografia de raios-X e a ressonância magnética nuclear (RMN). A ne
Publicado em: 2010
-
4. FMNL1 : caracterização de um novo gene humano relacionado com a familia das forminas
Formins are proteins that are involved in processes such as morphogenesis, embryonic differentiation, cytokinesis, cell polarity and survival. The formins are multidomain proteins that are conserved from plants to fungi and vertebrates. A search of the ORESTES database, generated from the Human Cancer Genome Project, identified 2 ESTs that were similar to th
Publicado em: 2006
-
5. Caracterização de disintegrinas de venenos viperídeos como ferramentas seletivas na detecção ou inibição da função de integrinas / Characterization of viper venom disintegrins as tools for detecting and inhibiting integrin function
Integrins are membrane proteins involved in biological processes such as embriogenesis, inflammation and platelet aggregation. The alteration of their expression pattem is related to pathological disorders such as thrombosis and cancer, making integrins suitable indicators of the progression of these diseases. Thus, the α2β1 integrin, which is expr
Publicado em: 2003
-
6. Annotation Transfer for Genomics: Measuring Functional Divergence in Multi-Domain Proteins
Annotation transfer is a principal process in genome annotation. It involves “transferring” structural and functional annotation to uncharacterized open reading frames (ORFs) in a newly completed genome from experimentally characterized proteins similar in sequence. To prevent errors in genome annotation, it is important that this process be robust and s
Cold Spring Harbor Laboratory Press.
-
7. Chemical synthesis and spontaneous folding of a multidomain protein: Anticoagulant microprotein S
Because of recent high-yield native ligation techniques, chemical synthesis of larger multidomain bioactive proteins is rapidly coming within reach. Here we describe the total chemical synthesis of a designed “microprotein S,” comprising the γ-carboxyglutamic acid-rich module, the thrombin-sensitive module, and the first epidermal growth factor-lik
The National Academy of Sciences.
-
8. DomIns: a web resource for domain insertions in known protein structures
Proteins can be formed by single or multiple domains. The process of recombination at the molecular level has generated a wide variety of multi-domain proteins with specific domain organization to cater to the functional requirements of an organism. The functional and structural costs of inserting a domain into another means that multi-domain proteins are us
Oxford University Press.
-
9. Symmetry, stability, and dynamics of multidomain and multicomponent protein systems
Symmetry is commonly observed in many biological systems. Here we discuss representative examples of the role of symmetry in structural molecular biology. Point group symmetries are observed in many protein oligomers whose three-dimensional atomic structures have been elucidated by x-ray crystallography. Approximate symmetry also occurs in multidomain p
The National Academy of Sciences of the USA.
-
10. Synaptic multiprotein complexes associated with5-HT2C receptors: a proteomic approach
Membrane-bound receptors such as tyrosine kinases and ionotropic receptors are associated with large protein networks structured by protein–protein interactions involving multidomain proteins. Although these networks have emerged as a general mechanism of cellular signalling, much less is known about the protein complexes associated with G-protein-coupled
Oxford University Press.
-
11. ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins
Multidomain proteins predominate in eukaryotic proteomes. Individual functions assigned to different sequence segments combine to create a complex function for the whole protein. While on-line resources are available for revealing globular domains in sequences, there has hitherto been no comprehensive collection of small functional sites/motifs comparable to
Oxford University Press.
-
12. Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily
The N-terminal regulatory domains of bacterial response regulator proteins catalyze phosphoryl transfer and function as phosphorylation-dependent regulatory switches to control the output activities of C-terminal effector domains. Structures of numerous isolated regulatory and effector domains have been determined. However, a detailed understanding of regula
American Society for Microbiology.