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Conserved Helix-Flanking Prolines Modulate Intrinsically Disordered Protein
Michael D Crabtree, Wade Borcherds, Anusha Poosapati, Sarah L Shammas, Gary W Daughdrill, Jane Clarke
Mar 26, 2018
Appropriate integration of cellular signals requires a delicate balance of ligand-target binding affinities. Increasing the level of residual structure in intrinsically disordered proteins (IDPs), which are overrepresented in...
Amino Acid Sequence Animals Binding Sites Cloning Molecular Conserved Sequence Escherichia coli Gene Expression Histone-Lysine N-Methyltransferase Humans Intrinsically Disordered Proteins Membrane Proteins Mice Models Molecular Mutation Myeloid-Lymphoid Leukemia Protein Phosphoproteins Proline Protein Binding Protein Conformation alpha-Helical Protein Folding Protein Interaction Domains and Motifs Recombinant Proteins Sequence Alignment Sequence Homology Amino Acid Tumor Suppressor Protein p53
Efficient and exact sampling of transition path ensembles on Markovian networks.
The problem of flickering trajectories in standard kinetic Monte Carlo (kMC) simulations prohibits sampling of the transition path ensembles (TPEs) on Markovian networks representing many slow dynamical processes of interest. In...
Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1.
James M Dunce, Amy E Milburn, Manickam Gurusaran, Irene da Cruz, Lee T Sen, Ricardo Benavente, Owen R Davies
Mar 02, 2020
Meiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere...
Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress.
The endoplasmic reticulum (ER) is a major site of protein synthesis, most strikingly in the specialized secretory cells of metazoans, which can produce their own weight in proteins daily. Cells possess a diverse machinery to...
A chain mechanism for flagellum growth.
Bacteria swim by means of long flagella extending from the cell surface. These are assembled from thousands of protein subunits translocated across the cell membrane by an export machinery at the base of each flagellum. Unfolded...
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.
IDP biophysics coupled folding and binding Electrostatics Kinetics phi-value protein dynamic protein electrostatics Protein Folding protein-protein interactions residual structure signaling Apoptosis Regulatory Proteins CREB-Binding Protein Cyclic AMP Response Element-Binding Protein Humans Hydrophobic and Hydrophilic Interactions Intrinsically Disordered Proteins Kinetics Molecular Dynamics Simulation Myeloid Cell Leukemia Sequence 1 Protein Protein Binding Protein Folding Protein Interaction Domains and Motifs Proto-Oncogene Proteins Signal Transduction Static Electricity Thermodynamics
Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.
Dennis Gessmann, Yong Hee Chung, Emily J Danoff, Ashlee M Plummer, Clifford W Sandlin, Nathan R Zaccai, Karen G Fleming
Jul 04, 2016
beta-barrel transmembrane protein membrane protein folding Bacterial Outer Membrane Proteins Biocatalysis Cell Membrane Escherichia coli Escherichia coli Proteins Kinetics Lipids Models Biological Periplasm Phenylalanine Phosphatidylethanolamines Phosphatidylglycerols Protein Folding Protein Structure Secondary
Generic membrane spanning features endow IRE1α with responsiveness to membrane aberrancy
Animals CHO Cells Cell Membrane Cricetulus DNA-Binding Proteins Endoplasmic Reticulum Endoplasmic reticulum stress Endoribonucleases Lipids Membrane Proteins Membranes Mutation Palmitic Acid Protein Domains Protein Folding Protein Serine-Threonine Kinases Signal Transduction Transcription Factors Unfolded Protein Response eIF-2 Kinase
Endoplasmic reticulum dysfunction in neurological disease.
Benoit D Roussel, Antonina J Kruppa, Elena Miranda, Damian C Crowther, David A Lomas, Stefan J Marciniak
May 18, 2018
Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral...
A method for partitioning the information contained in a protein sequence between its structure and function.
Proteins employ the information stored in the genetic code and translated into their sequences to carry out well-defined functions in the cellular environment. The possibility to encode for such functions is controlled by the...
Pressure and Chemical Unfolding of an α-Helical Bundle Protein
Cécile Dubois, Vicente J Planelles-Herrero, Camille Tillatte-Tripodi, Stéphane Delbecq, Léa Mammri, Elena M Sirkia, Virginie Ropars, Christian Roumestand, Philippe Barthe
Mar 31, 2021
When combined with NMR spectroscopy, high hydrostatic pressure is an alternative perturbation method used to destabilize globular proteins that has proven to be particularly well suited for exploring the unfolding energy...
NMR high hydrostatic pressure Protein Folding Thermodynamic stability α-helical bundle Adaptor Proteins Signal Transducing Humans Kinetics Magnetic Resonance Spectroscopy Models Molecular Protein Conformation Protein Conformation alpha-Helical Protein Denaturation Protein Domains Protein Unfolding Temperature Thermodynamics
Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry.
Lasse Staby, Katherine R Kemplen, Amelie Stein, Michael Ploug, Jane Clarke, Karen Skriver, Pétur O Heidarsson, Birthe B Kragelund
Sep 16, 2021
EF-hand Frequenin IDP NCS-1 Order–disorder interplay Protein Folding Amino Acid Sequence Binding Sites Carrier Proteins Humans Hydrophobic and Hydrophilic Interactions Intrinsically Disordered Proteins Kinetics Ligands Models Molecular Mutation Neuronal Calcium-Sensor Proteins Neuropeptides Protein Domains Protein Stability Thermodynamics
Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?
The prevailing current view of protein folding is the thermodynamic hypothesis, under which the native folded conformation of a protein corresponds to the global minimum of Gibbs free energy G. We question this concept and show...
Differential nuclear localization of complexes may underlie in vivo intrabody efficacy in Huntington's disease.
Huntington's disease intrabody nuclear polyglutamine single-chain Fv (scFv) Amino Acid Sequence Animals Cell Line Cell Nucleus Corpus Striatum Cytoplasm Female Huntington Disease Male Mice Molecular Sequence Data Peptides Protein Binding Protein Folding Rats Recombinant Fusion Proteins Single-Chain Antibodies Transfection
Structural insight into mitochondrial β-barrel outer membrane protein biogenesis.
Kathryn A Diederichs, Xiaodan Ni, Sarah E Rollauer, Istvan Botos, Xiaofeng Tan, Martin S King, Edmund RS Kunji, Jiansen Jiang, Susan K Buchanan
Jul 03, 2020
In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a...
Amino Acid Sequence Cryoelectron Microscopy detergents Fungal Proteins Mitochondria Mitochondrial Membrane Transport Proteins Mitochondrial Membranes Multiprotein Complexes Protein Biosynthesis Protein Conformation Protein Folding Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Sequence Homology Amino Acid Sordariales
Evaluation of template-based modeling in CASP13.
Performance in the template-based modeling (TBM) category of CASP13 is assessed here, using a variety of metrics. Performance of the predictor groups that participated is ranked using the primary ranking score that was developed...
Characterisation of denatured states of sensory rhodopsin II by solution-state NMR.
Sensory rhodopsin II (pSRII), a retinal-binding photophobic receptor from Natronomonas pharaonis, is a novel model system for membrane protein folding studies. Recently, the SDS-denatured states and the kinetics for reversible...
Evolved Minimal Frustration in Multifunctional Biomolecules.
Protein folding is often viewed in terms of a funneled potential or free energy landscape. A variety of experiments now indicate the existence of multifunnel landscapes, associated with multifunctional biomolecules. Here, we...
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