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1.
Phys Rev Lett ; 107(23): 236805, 2011 Dec 02.
Artigo em Inglês | MEDLINE | ID: mdl-22182117

RESUMO

We investigate the dependence of resonance energy transfer from Wannier-Mott excitons to an organic overlayer on exciton dimensionality. We exploit the excitonic potential disorder in a single quantum well to tune the balance between localized and free excitons by scaling the Boltzmann distribution of excitons through temperature. Theoretical calculations predict the experimentally observed temperature dependence of resonance energy transfer and allow us to quantify the contribution of localized and free excitons. We show that free excitons can undergo resonance energy transfer with an order of magnitude higher rate compared to localized excitons, emphasizing the potential of hybrid optoelectronic devices utilizing resonance energy transfer as a means to overcome charge transfer related limitations.

2.
Nat Med ; 18(1): 71-3, 2011 Dec 11.
Artigo em Inglês | MEDLINE | ID: mdl-22157680

RESUMO

Congenital disorder of glycosylation-Ia (CDG-Ia, also known as PMM2-CDG) is caused by mutations in the gene that encodes phosphomannomutase 2 (PMM2, EC 5.4.2.8) leading to a multisystemic disease with severe psychomotor and mental retardation. In a hypomorphic Pmm2 mouse model, we were able to overcome embryonic lethality by feeding mannose to pregnant dams. The results underline the essential role of glycosylation in embryonic development and may open new treatment options for this disease.


Assuntos
Defeitos Congênitos da Glicosilação/metabolismo , Defeitos Congênitos da Glicosilação/prevenção & controle , Desenvolvimento Embrionário/efeitos dos fármacos , Manose/uso terapêutico , Fosfotransferases (Fosfomutases)/genética , Cuidado Pré-Natal/métodos , Animais , Defeitos Congênitos da Glicosilação/genética , Modelos Animais de Doenças , Feminino , Genes Letais , Glicosilação/efeitos dos fármacos , Humanos , Camundongos , Gravidez
3.
J Am Chem Soc ; 133(2): 279-85, 2011 Jan 19.
Artigo em Inglês | MEDLINE | ID: mdl-21155557

RESUMO

Intramolecular distances in proteins and other biomolecules can be studied in living cells by means of fluorescence resonance energy transfer (FRET) in steady-state or pulsed-excitation experiments. The major uncertainty originates from the unknown orientation between the optical dipole moments of the fluorescent markers, especially when the molecule undergoes thermal fluctuations in physiological conditions. We introduce a statistical method based on the von Mises-Fisher distribution for the interpretation of fluorescence decay dynamics in donor-acceptor FRET pairs that allows us to retrieve both the orientation and the extent of directional fluctuations of the involved dipole moments. We verify the method by applying it to donor-acceptor pairs controllably attached to DNA helices and find that common assumptions such as complete rotational freedom or fully hindered rotation of the dipoles fail a physical interpretation of the fluorescence decay dynamics. This methodology is applicable in single-molecule and ensemble measurements of FRET to derive more accurate distance estimates from optical experiments, without the need for more complex and expensive NMR studies.


Assuntos
Transferência Ressonante de Energia de Fluorescência , Corantes Fluorescentes/química , DNA/química , Fluorescência , Modelos Moleculares , Estrutura Molecular
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