Results 221 to 230 of about 302,602 (263)
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Protein concentration with single-pass tangential flow filtration (SPTFF)
Journal of Membrane Science, 2011Abstract This paper presents a novel Cadence™ single-pass tangential flow filtration (SPTFF) process for protein concentration, operating in a continuous mode. The main advantages of the SPTFF technology have been highlighted in a benchmark comparison test versus conventional TFF.
Catherine Casey +4 more
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NMR structure of a full‐length single‐pass membrane protein NRADD
Proteins: Structure, Function and Bioinformatics, 2019AbstractStructural study of any single‐pass membrane protein is both an important and challenging task. In this report, we present the structure of a neurotrophin receptor‐alike death‐domain protein. The structure and dynamics of the protein was investigated by conventional nuclear magnetic resonance techniques in the solution of phospholipid bicelles.
Kirill D Nadezhdin +2 more
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Multi-pass nanopore for single-molecule protein sequencing
Nature MethodsArunima Singh, Singh Arunima
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Effect of Gastric By‐pass on Dietary Protein Bioavailability and Protein Anabolism in Rats
The FASEB Journal, 2017Introduction Bariatric surgery is an efficient treatment of massive obesity but it can trigger nutritional deficiencies, especially regarding vitamins and proteins. Protein wasting may be observed although there are large prevalence variations in the literature.
Gaudichon, Claire +8 more
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Structural insights into the membrane chaperones for multi-pass membrane protein biogenesis
Current Opinion in Structural Biology, 2023Certain transmembrane α-helices of multi-pass membrane proteins line substrate transport paths or catalytic pockets and, therefore, are partially hydrophilic. Sec61 alone is insufficient to insert these less hydrophobic segments into the membrane and needs to work with dedicated membrane chaperones. Three such membrane chaperones have been described in
Lin Bai, Huilin Li
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Fast prediction and visualization of protein binding pockets with PASS
Journal of Computer-Aided Molecular Design, 2000PASS (Putative Active Sites with Spheres) is a simple computational tool that uses geometry to characterize regions of buried volume in proteins and to identify positions likely to represent binding sites based upon the size, shape, and burial extent of these volumes.
G. Patrick Brady Jr. +1 more
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White collar proteins: PASsing the light signal in Neurospora crassa
Trends in Microbiology, 1997The filamentous fungus Neurospora crassa is an excellent paradigm for the study of blue light signal transduction. The isolation and characterization of the genes for two central regulators of the blue light response, white collar-1 and white collar-2, have begun to shed light on the mechanism of blue light signal transduction in fungi.
BALLARIO, Paola, MACINO, Giuseppe
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Requirements for band-pass activation of Ca2+-sensitive proteins such as NFAT
Biophysical Chemistry, 2019Several proteins are sensitive to frequency-modulated oscillations of calcium levels. Most of them exhibit increased activities for faster frequencies, a characteristic here referred to as high-pass activation. In contrast, the transcription factor NFAT is optimally activated at a specific frequency, a behaviour we call band-pass activation.
Arne, Schoch, Jürgen, Pahle
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Recombinant clotting protein passes trials
Chemical & Engineering News Archive, 1991An international clinical study of recombinant blood clotting factor VIII in 107 hemophiliacs indicates that the genetically engineered material is at least as effective as protein isolated from blood plasma. This result will help pave the way for approval by the Food & Drug Administration of a hemophilia therapy free of risk of contamination by AIDS ...
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