Results 81 to 90 of about 734,673 (317)

Conformational variability of loops in the SARS-CoV-2 spike protein [PDF]

arXiv, 2021
The SARS-CoV-2 spike (S) protein facilitates viral infection, and has been the focus of many structure determination efforts. Its flexible loop regions are known to be involved in protein binding and may adopt multiple conformations. This paper identifies the S protein loops and studies their conformational variability based on the available Protein ...
arxiv  

Ion channel function of polycystin‐2/polycystin‐1 heteromer revealed by structure‐guided mutagenesis

FEBS Letters, EarlyView.
Mutations in polycystin‐1 (PC1) or polycystin‐2 (PC2) cause autosomal‐dominant polycystic kidney disease (ADPKD). We generated a novel gain‐of‐function PC2/PC1 heteromeric ion channel by mutating pore‐blocking residues. Moreover, we demonstrated that PC2 will preferentially assemble with PC1 to form heteromeric complexes when PC1 is co‐expressed ...
Tobias Staudner, Juthamas Khamseekaew, M. Gregor Madej, Linda Geiges, Bardha Azemi, Christine Ziegler, Christoph Korbmacher, Alexandr V. Ilyaskin   +7 more
wiley   +1 more source

The role of C-terminal helix in the conformational transition of an arginine binding protein

Journal of Structural Biology: X, 2022
The thermotoga maritima arginine binding protein (TmArgBP) is a periplasmic binding protein that has a short helix at the C-terminal end (CTH), which is swapped between the two chains. We apply a coarse-grained structure-based model (SBM) and all-atom MD
Vinothini Santhakumar, Nahren Manuel Mascarenhas   +1 more
doaj  

Single-Molecule Study of Proteins by Biological Nanopore Sensors

Sensors, 2014
Nanopore technology has been developed for detecting properties of proteins through monitoring of ionic current modulations as protein passes via a nanosize pore.
Dongmei Wu, Sheng Bi, Liyu Zhang, Jun Yang   +3 more
doaj   +1 more source

Space Layout of Low-entropy Hydration Shells Guides Protein Binding [PDF]

arXiv, 2022
Protein-protein binding enables orderly and lawful biological self-organization, and is therefore considered a miracle of nature. Protein-protein binding is steered by electrostatic forces, hydrogen bonding, van der Waals force, and hydrophobic interactions.
arxiv  

Autophagy in cancer and protein conformational disorders

FEBS Letters, EarlyView.
Autophagy plays a crucial role in numerous biological processes, including protein and organelle quality control, development, immunity, and metabolism. Hence, dysregulation or mutations in autophagy‐related genes have been implicated in a wide range of human diseases.
Sergio Attanasio
wiley   +1 more source

Integrity of H1 helix in prion protein revealed by molecular dynamic simulations to be especially vulnerable to changes in the relative orientation of H1 and its S1 flank

, 2009
In the template-assistance model, normal prion protein (PrPC), the pathogenic cause of prion diseases such as Creutzfeldt-Jakob (CJD) in human, Bovine Spongiform Encephalopathy (BSE) in cow, and scrapie in sheep, converts to infectious prion (PrPSc ...
A Aguzzi, A Aguzzi, A Barducci, A Onufriev, C Guilbert, Chih-Yuan Tseng, Chun-Ping Yu, DA Case, DA Harris, E Lindahl, E Malolepsza, F Eghiaian, GJ Sharman, GS Jackson, H. C. Lee, HJC Berendsen, J Castilla, J Watzlawik, J Ziegler, JP Ryckaert, KM Pan, L Calzolai, M Horiuchi, ML DeMarco, ML DeMarco, MP Morrissey, N Guex, P Derreumaux, P Tompa, R Riek, RI Dima, S Megy, S Santini, S Santini, SA Kozin, SB Prusiner, T Muramoto, W Kabsch, WQ Zou, Y Levy, Y Levy   +40 more
core   +1 more source

Protonophore activity of short‐chain fatty acids induces their intracellular accumulation and acidification

FEBS Letters, EarlyView.
The protonated form of butyrate, as well as other short‐chain fatty acids (SCFAs), is membrane permeable. In acidic extracellular environments, this can lead to intracellular accumulation of SCFAs and cytosolic acidification. This phenomenon will be particularly relevant in acidic environments such as the large intestine or tumor microenvironments ...
Muwei Jiang, Frans Bianchi, Geert van den Bogaart   +2 more
wiley   +1 more source

Selected-fit versus induced-fit protein binding: Kinetic differences and mutational analysis [PDF]

arXiv, 2008
The binding of a ligand molecule to a protein is often accompanied by conformational changes of the protein. A central question is whether the ligand induces the conformational change (induced-fit), or rather selects and stabilizes a complementary conformation from a pre-existing equilibrium of ground and excited states of the protein (selected-fit ...
arxiv  

Brucella NyxA and NyxB dimerization enhances effector function during infection

FEBS Letters, EarlyView.
Brucella abortus thrives inside cells thanks to the translocation of effector proteins that fine‐tune cellular functions. NyxA and NyxB are two effectors that destabilize the nucleolar localization of their host target, SENP3. We show that the Nyx proteins directly interact with each other and that their dimerization is essential for their function ...
Lison Cancade‐Veyre, Arthur Louche, Francine C. A. Gérard, Laurent Terradot, Suzana P. Salcedo   +4 more
wiley   +1 more source