نتایج جستجو برای: 015g for 475

تعداد نتایج: 10354124  

Journal: :The Biochemical journal 1995
O Shimomura

Aequorin emits light in the presence of Ca2+, decomposing into apoaequorin, coelenteramide and CO2. Semisynthetic aequorins, produced by replacing the coelenterazine moiety in aequorin with analogues of coelenterazine, showed widely different sensitivities to Ca2+ as well as certain spectral variations. A group of semisynthetic aequorins, e-type aequorins, showed bimodal luminescence, with peak...

Journal: :The Journal of biological chemistry 2003
Izabela Sokal Guang Hu Yan Liang Muling Mao Theodore G Wensel Krzysztof Palczewski

Inactivation of the visual G-protein transducin by GTP hydrolysis is regulated by the GTPase-accelerating protein (GAP) RGS9-1. Regulation of RGS9-1 itself is poorly understood, but we found previously that it is subject to a light- and Ca(2+)-sensitive phosphorylation on Ser(475). Because there are much higher RGS9-1 levels in cones than in rods, we investigated whether Ser(475) is phosphoryla...

Journal: :International Astronomical Union Colloquium 1982

Journal: :Science 2012
Christoph C Pradzynski Richard M Forck Thomas Zeuch Petr Slavíček Udo Buck

The number of water molecules needed to form the smallest ice crystals has proven challenging to pinpoint experimentally. This information would help to better understand the hydrogen-bonding interactions that account for the macroscopic properties of water. Here, we report infrared (IR) spectra of precisely size-selected (H(2)O)(n) clusters, with n ranging from 85 to 475; sodium doping and ass...

2000
Philippe Ferrara Joannis Apostolakis Amedeo Caflisch

The usefulness of targeted molecular dynamics (TMD) for the simulation of large conformational transitions is assessed in this work on the unfolding process of chymotrypsin inhibitor 2 (CI2). In TMD the force field is supplemented with a harmonic restraint which promotes either the increase of the conformational distance from the native state or the decrease of the distance from a target unfold...

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