Marc Siggel
Max Planck Society
Globular proteinChemistryPhospholipid scramblaseRotational diffusionMolecular dynamics
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Publications 3
#1Xudong Wu (HHMI: Howard Hughes Medical Institute)H-Index: 2
#2Marc Siggel (MPG: Max Planck Society)H-Index: 1
Last. Tom A. Rapoport (HHMI: Howard Hughes Medical Institute)H-Index: 95
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INTRODUCTION Protein homeostasis in the endoplasmic reticulum (ER) is maintained by a quality control system. When a newly synthesized ER protein misfolds, it is ultimately retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome, a pathway referred to as ER-associated protein degradation (ERAD). ERAD alleviates cytotoxic stress imposed by protein misfolding and is implicated in numerous diseases. ERAD is found in all eukaryotic cells but is best studied for the ERAD...
2 CitationsSource
#1Marc Siggel (MPG: Max Planck Society)H-Index: 1
#2Ramachandra M. Bhaskara (MPG: Max Planck Society)H-Index: 8
Last. Gerhard Hummer (Goethe University Frankfurt)H-Index: 77
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The cell membrane and many organellar membranes are asymmetric and highly curved. In experiments, it is challenging to reconstitute and characterize membranes that differ in the lipid composition of their leaflets. Here we use molecular dynamics simulations to study the large-scale membrane shape changes associated with lipid shuttling between asymmetric leaflets. We exploit leaflet asymmetry to create a stable, near-spherical vesicle bud connected to a flat bilayer under periodic boundary condi...
#1Sören von Bülow (MPG: Max Planck Society)H-Index: 1
#2Marc Siggel (MPG: Max Planck Society)H-Index: 1
Last. Gerhard Hummer (Goethe University Frankfurt)H-Index: 77
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We develop a detailed description of protein translational and rotational diffusion in concentrated solution on the basis of all-atom molecular dynamics simulations in explicit solvent. Our systems contain up to 540 fully flexible proteins with 3.6 million atoms. In concentrated protein solutions (100 mg/mL and higher), the proteins ubiquitin and lysozyme, as well as the protein domains third IgG-binding domain of protein G and villin headpiece, diffuse not as isolated particles, but as members ...
1 CitationsSource