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Methods for Engineering Binders to Multi-Pass Membrane Proteins

Bioengineering, 2023
Numerous potential drug targets, including G-protein-coupled receptors and ion channel proteins, reside on the cell surface as multi-pass membrane proteins. Unfortunately, despite advances in engineering technologies, engineering biologics against multi-pass membrane proteins remains a formidable task.
Zhilei Chen
exaly   +4 more sources

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Fast Prediction and Visualization of Protein Binding Pockets With PASS

Journal of Computer-Aided Molecular Design, 2000
PASS (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.
Pieter Stouten
exaly   +3 more sources

Detecting Folding Intermediates of a Protein as It Passes Through the Bacterial Translocation Channel [PDF]

Cell, 2009
Most bacterial exported proteins cross the cytoplasmic membrane as unfolded polypeptides. However, little is known about how they fold during or after this process due to the difficulty in detecting folding intermediates. Here we identify cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA,
Hiroshi Kadokura, Jon Beckwith
exaly   +3 more sources

Effect of Gastric By‐pass on Dietary Protein Bioavailability and Protein Anabolism in Rats

The FASEB Journal, 2017
Introduction 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, Tessier, Romain, Ribeiro-Parenti, Lara, Ouafa, Bruneau, Cavin, Jean-Baptiste, Khodorova, Nadezda, Bado, André, Tomé, Daniel, Le Gall, Maude   +8 more
openaire   +3 more sources

Structural insights into the membrane chaperones for multi-pass membrane protein biogenesis

Current Opinion in Structural Biology, 2023
Certain 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
openaire   +2 more sources

Multi-Pass Nanopore for Single-Molecule Protein Sequencing

Nature Methods
Arunima Singh
exaly   +3 more sources

Structural biology - Pass the protein

2007
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Jean-Francois Trempe, Jane Endicott
openaire   +1 more source