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1.
Radiat Prot Dosimetry ; 177(1-2): 21-25, 2017 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-29036460

RESUMO

An automatic measuring apparatus called exhalometer for measurement of the radon exhalation rate from soil is introduced. It consists of a pneumatic driven accumulation chamber with an open bottom, a PC-based control system, six Lucas cells for radon measurement and sensors for environmental parameters. It allows moving the accumulation chamber and hereby opening or closing it. The exhalation rate is determined through the increase of radon in the accumulation chamber. For studying exhalation and the affecting factors, the exhalometer was placed at an undisturbed meadow for the entire year of 2015. The daily radon exhalation rate ranges from 2.5 to 50.7 Bq m-2 h-1 with an average of 25.3 Bq m-2 h-1. The exhalation rate shows daily and seasonal variations with its maximum in the afternoon and in spring. The dependence on several environmental parameters is discussed. The stable performance indicates the system's fitness for long-term measurements.


Assuntos
Exposição Ambiental/análise , Monitoramento de Radiação/instrumentação , Radônio/análise , Poluentes Radioativos do Solo/análise , Desenho de Equipamento , Estações do Ano
2.
Proc Natl Acad Sci U S A ; 114(23): 6040-6045, 2017 06 06.
Artigo em Inglês | MEDLINE | ID: mdl-28533394

RESUMO

Owing to the cooperativity of protein structures, it is often almost impossible to identify independent subunits, flexible regions, or hinges simply by visual inspection of static snapshots. Here, we use single-molecule force experiments and simulations to apply tension across the substrate binding domain (SBD) of heat shock protein 70 (Hsp70) to pinpoint mechanical units and flexible hinges. The SBD consists of two nanomechanical units matching 3D structural parts, called the α- and ß-subdomain. We identified a flexible region within the rigid ß-subdomain that gives way under load, thus opening up the α/ß interface. In exactly this region, structural changes occur in the ATP-induced opening of Hsp70 to allow substrate exchange. Our results show that the SBD's ability to undergo large conformational changes is already encoded by passive mechanics of the individual elements.


Assuntos
Trifosfato de Adenosina/metabolismo , Proteínas de Choque Térmico HSP70/química , Proteínas de Choque Térmico HSP70/metabolismo , Regulação Alostérica , Sítio Alostérico , Sequência de Aminoácidos , Escherichia coli/metabolismo , Proteínas de Escherichia coli/metabolismo , Proteínas de Choque Térmico HSP70/ultraestrutura , Cinética , Microscopia de Força Atômica/métodos , Simulação de Dinâmica Molecular , Ligação Proteica , Conformação Proteica , Domínios Proteicos , Especificidade por Substrato
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