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Amsterdam 2004 - Theoretical Biology & Bioinformatics
Amsterdam 2004 - Theoretical Biology & Bioinformatics

... rfbB / rffG ...
What You Need To Know about ENZYMES ???
What You Need To Know about ENZYMES ???

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Solution Key 7.013 Practice Exam 2
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... b) You want to study another nuclear protein, TF-2 in mouse muscle cells. You identify a mutant cell line, which shows a cytosolic location of TF-2 in muscle cells. i. Name a stretch of amino acid sequence that the TF-2 in mutant muscle cell line lacks. Nuclear localization sequence ii. In the wild- ...
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College 1 - Xray and NMR
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coIP就是co-immunoprecipitation,假如有两种蛋白质A,B相互作用
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... identify using physical methods like pull-down assays because the complex may dissociate during the assay. Since transient interactions occur during transport or as part of enzymatic processes, they often require cofactors and energy via nucleotide triphosphates hydrolysis. Incorporating cofactors a ...
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... (Supplemental Fig. S1). To gain insight into the distribution of Why1 within the plastid, stroma and membrane fractions were prepared from chloroplasts. By immunoblot analysis the major part of Why1 was detected in the stroma while a minor part was found in the membrane fraction (Fig. 2C). For analy ...
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Gene Products annotated

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Gene Section PA2G4 (proliferation associated 2G4, 38kDa) -
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... The two forms have been demonstrated to be the result of alternative splicing (Liu et al., 2006) or usage of alternative translation initiation sites (Xia et al., 2001). Amino acids 1-48 are required for nucleolar localization and the C terminal domain (aa 364-394) is required for interactions with ...
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... Cell Organelles Graphic Organizer Visit www.cellsalive.com/cells/cell_model.htm and begin by choosing Animal Cell or Plant Cell. Label the diagrams with just the name of the organelle. Then move on to reading the description of each organelle and filling in the information needed (bullet points are ...
bchm6280_16_ex5a
bchm6280_16_ex5a

... 4. You can download the data as sequences or tab-delimited data that can be imported into Excel. Save the exported data as a Excel workbook, with each gene list as a separate worksheet. Spend some time looking at your lists. When choosing a gene for follow-up studies, at least within the context of ...
Exercise1_2015
Exercise1_2015

... unlimited search for cytochrome c oxidase in the OMIM database. Repeat the query for “cytochrome c oxidase” as a term. Which search is more restrictive? Limit the retrieved entries only to those with gene location on chromosomes 4, 6 and 19. How many records have you retrieved? What is the chromosom ...
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Protein moonlighting



Protein moonlighting (or gene sharing) is a phenomenon by which a protein can perform more than one function. Ancestral moonlighting proteins originally possessed a single function but through evolution, acquired additional functions. Many proteins that moonlight are enzymes; others are receptors, ion channels or chaperones. The most common primary function of moonlighting proteins is enzymatic catalysis, but these enzymes have acquired secondary non-enzymatic roles. Some examples of functions of moonlighting proteins secondary to catalysis include signal transduction, transcriptional regulation, apoptosis, motility, and structural.Protein moonlighting may occur widely in nature. Protein moonlighting through gene sharing differs from the use of a single gene to generate different proteins by alternative RNA splicing, DNA rearrangement, or post-translational processing. It is also different from multifunctionality of the protein, in which the protein has multiple domains, each serving a different function. Protein moonlighting by gene sharing means that a gene may acquire and maintain a second function without gene duplication and without loss of the primary function. Such genes are under two or more entirely different selective constraints.Various techniques have been used to reveal moonlighting functions in proteins. The detection of a protein in unexpected locations within cells, cell types, or tissues may suggest that a protein has a moonlighting function. Furthermore, sequence or structure homology of a protein may be used to infer both primary function as well as secondary moonlighting functions of a protein.The most well-studied examples of gene sharing are crystallins. These proteins, when expressed at low levels in many tissues function as enzymes, but when expressed at high levels in eye tissue, become densely packed and thus form lenses. While the recognition of gene sharing is relatively recent—the term was coined in 1988, after crystallins in chickens and ducks were found to be identical to separately identified enzymes—recent studies have found many examples throughout the living world. Joram Piatigorsky has suggested that many or all proteins exhibit gene sharing to some extent, and that gene sharing is a key aspect of molecular evolution. The genes encoding crystallins must maintain sequences for catalytic function and transparency maintenance function.Inappropriate moonlighting is a contributing factor in some genetic diseases, and moonlighting provides a possible mechanism by which bacteria may become resistant to antibiotics.
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