On the origin of the boson peak in globular proteins

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We consider the problem of compressing an information source when a correlated one is available as side information only at the decoder side, which is a special case of the distributed source coding problem in information theory. In particular, we consider ...

Proteins control nearly every facet of life on a molecular level. Proteins are formed from linear strings of amino acids, which fold into three-dimensional structures that can enact functions. Evolution has created highly efficient proteins in diverse fold ...

Structure determination of amorphous materials remains challenging, owing to the disorder inherent to these materials. Nuclear magnetic resonance (NMR) powder crystallography is a powerful method to determine the structure of molecular solids, but disorder ...

Understanding and describing the dynamics of proteins is one of the major challenges in biology. Here, we use multifield variable-temperature NMR longitudinal relaxation (R-1) measurements to determine the hierarchical activation energies of motions of fou ...

S-acylation is one of the most frequent posttranslational modifications that regulates diverse cellular processes. Anwar and van der Goot discuss the complexity and disease implications of this highly regulated reversible lipidation. ...

Continuous assessment of transferable forcefields for molecular simulations is essential to identify their weaknesses and direct improvement efforts. The latest efforts focused on better describing disordered proteins while retaining proper description of ...

In the past decade, optical diffraction tomography has gained a lot of attention for its ability to create label-free three-dimensional (3D) images of the refractive index distribution of biological samples using scattered fields measured through holograph ...

Resolution in proton solid state magic angle sample spinning (MAS) NMR is limited by the intrinsically imperfect nature of coherent averaging induced by either MAS or multiple pulse sequence methods. Here, we suggest that instead of optimizing and perfecti ...

We study the spectra of non-regular semisimple elements in irreducible representations of simple algebraic groups. More precisely, we prove that if G is a simply connected simple linear algebraic group and φ : G → GL(V ) is a non-trivial irreducible repres ...

Knowledge-based approaches use the statistics collected from protein data-bank structures to estimate effective interaction potentials between amino acid pairs. Empirical relations are typically employed that are based on the crucial choice of a reference ...

Imaging of proteins at the single-molecule level can reveal conformational variability, which is essential for the understanding of biomolecules. To this end, a biologically relevant state of the sample must be retained during both sample preparation and i ...

Understanding how proteins fold into their native structure is a fundamental problem in biophysics, crucial for protein design. It has been hypothesized that the formation of a molten globule intermediate precedes folding to the native conformation of glob ...

The sheer size of the protein sequence space is massive: a protein of 100 residues can have 20^100 possible sequence combinations; and knowing that this exceeds the number of atoms in the universe, the chance of randomly discovering a stable new sequence w ...

The present relates to a method for generating variants of a protein based on a native protein regulated by allosteric pathway, the method comprising: - i) providing 3D structures of the native protein; - ii) identifying at least one pair of coupled allost ...

On the origin of the boson peak in globular proteins

Chattez avec Graph Search

Neural Distributed Image Compression with Cross-Attention Feature Alignment

De novo designed proteins: a study in engineering novel folds and functions

Atomic-level structure determination of amorphous molecular solids by NMR

Similarities and Differences among Protein Dynamics Studied by Variable Temperature Nuclear Magnetic Resonance Relaxation

Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications

Assessment of transferable forcefields for protein simulations attests improved description of disordered states and secondary structure propensities, and hints at multi-protein systems as the next challenge for optimization

Exploring Novel Modalities for Optical Diffraction Tomography

Pure Isotropic Proton Solid State NMR

Spectra of non-regular elements in irreducible representations of simple algebraic groups

Statistical potentials from the Gaussian scaling behaviour of chain fragments buried within protein globules

Low-energy electron holography imaging of conformational variability of single-antibody molecules from electrospray ion beam deposition

Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy

Towards automating de novo protein design for novel functionalities: controlling protein folds and protein-protein interactions

Method for generating variants of a protein