8 resultados para Fp Plaque Variants

em Digital Commons at Florida International University


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Sabrena O'Keefe giving speech while holding the time capsule plaque. Also pictured: Pablo Haspel, BBC SGA President, BBC Campus Laura Farinas, SGA President, MMC Campus The Annual FIU Student Leadership Summit is held each February on the Biscayne Bay Campus. The Summit is a one-day conference for current student leaders. The Summit offers our students the opportunity to learn from the vast expertise of our faculty and administrators, to share their leadership experiences with each other and to establish a network of support and cooperation within the university. On Feb. 2, 2013, we celebrated the 10th anniversary of holding the Student Leadership Summit. In honor of this occasion, we buried a time capsule containing materials from the day as well as messages from participants to the participants of 2023 when the time capsule is to be opened.

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Time capsule burial plaque before placed on burial site. The Annual FIU Student Leadership Summit is held each February on the Biscayne Bay Campus. The Summit is a one-day conference for current student leaders. The Summit offers our students the opportunity to learn from the vast expertise of our faculty and administrators, to share their leadership experiences with each other and to establish a network of support and cooperation within the university. On Feb. 2, 2013, we celebrated the 10th anniversary of holding the Student Leadership Summit. In honor of this occasion, we buried a time capsule containing materials from the day as well as messages from participants to the participants of 2023 when the time capsule is to be opened.

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Sabrena O'Keefe giving speech while holding the time capsule plaque. Also pictured: Pablo Haspel, BBC SGA President, BBC Campus Laura Farinas, SGA President, MMC Campus The Annual FIU Student Leadership Summit is held each February on the Biscayne Bay Campus. The Summit is a one-day conference for current student leaders. The Summit offers our students the opportunity to learn from the vast expertise of our faculty and administrators, to share their leadership experiences with each other and to establish a network of support and cooperation within the university. On Feb. 2, 2013, we celebrated the 10th anniversary of holding the Student Leadership Summit. In honor of this occasion, we buried a time capsule containing materials from the day as well as messages from participants to the participants of 2023 when the time capsule is to be opened.

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The buried time capsule and plaque. The Annual FIU Student Leadership Summit is held each February on the Biscayne Bay Campus. The Summit is a one-day conference for current student leaders. The Summit offers our students the opportunity to learn from the vast expertise of our faculty and administrators, to share their leadership experiences with each other and to establish a network of support and cooperation within the university. On Feb. 2, 2013, we celebrated the 10th anniversary of holding the Student Leadership Summit. In honor of this occasion, we buried a time capsule containing materials from the day as well as messages from participants to the participants of 2023 when the time capsule is to be opened.

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Fluorescent proteins (FPs) are extremely valuable biochemical markers which have found a wide range of applications in cellular and molecular biology research. The monomeric variants of red fluorescent proteins (RFPs), known as mFruits, have been especially valuable for in vivo applications in mammalian cell imaging. Fluorescent proteins consist of a chromophore caged in the beta-barrel protein scaffold. The photophysical properties of an FP is determined by its chromophore structure and its interactions with the protein barrel. Application of hydrostatic pressure on FPs results in the modification of the chromophore environment which allows a systematic study of the role of the protein-chromophore interactions on photophysical properties of FPs. Using Molecular Dynamics (MD) computer simulations, I investigated the pressure induced structural changes in the monomeric variants mCherry, mStrawberry, and Citrine. The results explain the molecular basis for experimentally observed pressure responses among FP variants. It is found that the barrel flexibility, hydrogen bonding interactions and chromophore planarity of the FPs can be correlated to their contrasting photophysical properties at vaious pressures. I also investigated the oxygen diffusion pathways in mOrange and mOrange2 which exhibit marked differences in oxygen sensitivities as well as photostability. Such computational identifications of structural changes and oxygen diffusion pathways are important in guiding mutagenesis efforts to design fluorescent proteins with improved photophysical properties.

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Gene-based tests of association are frequently applied to common SNPs (MAF>5%) as an alternative to single-marker tests. In this analysis we conduct a variety of simulation studies applied to five popular gene-based tests investigating general trends related to their performance in realistic situations. In particular, we focus on the impact of non-causal SNPs and a variety of LD structures on the behavior of these tests. Ultimately, we find that non-causal SNPs can significantly impact the power of all gene-based tests. On average, we find that the “noise” from 6–12 non-causal SNPs will cancel out the “signal” of one causal SNP across five popular gene-based tests. Furthermore, we find complex and differing behavior of the methods in the presence of LD within and between non-causal and causal SNPs. Ultimately, better approaches for a priori prioritization of potentially causal SNPs (e.g., predicting functionality of non-synonymous SNPs), application of these methods to sequenced or fully imputed datasets, and limited use of window-based methods for assigning inter-genic SNPs to genes will improve power. However, significant power loss from non-causal SNPs may remain unless alternative statistical approaches robust to the inclusion of non-causal SNPs are developed.

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Fluorescent proteins (FPs) are extremely valuable biochemical markers which have found a wide range of applications in cellular and molecular biology research. The monomeric variants of red fluorescent proteins (RFPs), known as mFruits, have been especially valuable for in vivo applications in mammalian cell imaging. Fluorescent proteins consist of a chromophore caged in the beta-barrel protein scaffold. The photophysical properties of an FP is determined by its chromophore structure and its interactions with the protein barrel. Application of hydrostatic pressure on FPs results in the modification of the chromophore environment which allows a systematic study of the role of the protein-chromophore interactions on photophysical properties of FPs. Using Molecular Dynamics (MD) computer simulations, I investigated the pressure induced structural changes in the monomeric variants mCherry, mStrawberry, and Citrine. The results explain the molecular basis for experimentally observed pressure responses among FP variants. It is found that the barrel flexibility, hydrogen bonding interactions and chromophore planarity of the FPs can be correlated to their contrasting photophysical properties at vaious pressures. I also investigated the oxygen diffusion pathways in mOrange and mOrange2 which exhibit marked differences in oxygen sensitivities as well as photostability. Such computational identifications of structural changes and oxygen diffusion pathways are important in guiding mutagenesis efforts to design fluorescent proteins with improved photophysical properties.