Concept

Protein tertiary structure

Related publications (880)

Structure of fully protonated proteins by proton-detected magic-angle spinning NMR

Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we sh ...

National Academy of Sciences2016

Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I

Henning Paul-Julius Stahlberg

High-density lipoprotein (HDL) particles are cholesterol and lipid transport containers. Mature HDL particles destined for the liver develop through the formation of intermediate discoidal HDL particles, which are the primary acceptors for cholesterol. Her ...

Springer Nature2016

Molecular Effects of Concentrated Solutes on Protein Hydration, Dynamics, and Electrostatics

Matteo Dal Peraro, Luciano Andres Abriata, Enrico Spiga

Most studies of protein structure and function are performed in dilute conditions, but proteins typically experience high solute concentrations in their physiological scenarios and biotechnological applications. High solute concentrations have well-known e ...

Cell Press2016

PyMOL and Inkscape Bridge the Data and the Data Visualization

Horst Vogel, Shuguang Yuan

Structural biology has come a long way, from being a niche interest of specialists to where we are today, with over 127,500 biomolecular structures available in the Protein Data Bank (PDB) as of the writing of this letter. The two main factors that have be ...

Elsevier2016

A method for building a structure containing living cells

Matthias Lütolf, Andrea Negro

A composition comprising a first material and a second material, wherein said first material is cross-linkable by a first cross- linking reaction and said second material is cross-linkable by a second cross-linking reaction, wherein said first cross-linkin ...

2016

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Pierre Goloubinoff, Andrija Finka

Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can bind a ...

Annual Reviews2016

Thin-film-specific elastic effects in ferroelectric domain structures

Konstantin Shapovalov

An essential feature of ferroelectric thin films is the presence in them of domain structures. In order to efficiently implement ferroelectric films into potential new ferroelectrics-based devices, it is of high interest to understand the behaviour of doma ...

EPFL2016

Automated longitudinal monitoring of in vivo protein aggregation in neurodegenerative disease C. elegans models

Johan Auwerx, Martinus Gijs, Thomas Lehnert, Matteo Cornaglia, Laurent Mouchiroud, Vincenzo Sorrentino, Govindan Narayanan Krishnamani

Background: While many biological studies can be performed on cell-based systems, the investigation of molecular pathways related to complex human dysfunctions - e.g. neurodegenerative diseases - often requires long-term studies in animal models. The nemat ...

BioMed Central2016

Distributed computation of generalized Nash equilibria in quadratic aggregative games with affine coupling constraints

Maryam Kamgarpour, John Lygeros

We analyse deterministic aggregative games, with large but finite number of players, that are subject to both local and coupling constraints. Firstly, we derive sufficient conditions for the existence of a generalized Nash equilibrium, by using the theory ...

IEEE2016

The Principles of Ligand Specificity on beta-2-adrenergic receptor

Shuguang Yuan

G protein-coupled receptors are recognized as one of the largest families of membrane proteins. Despite sharing a characteristic seven-transmembrane topology, G protein-coupled receptors regulate a wide range of cellular signaling pathways in response to v ...

Nature Publishing Group2016

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