Results 41 to 50 of about 6,420,371 (402)

Structural interrogation of phosphoproteome identified by mass spectrometry reveals allowed and disallowed regions of phosphoconformation [PDF]

open access: yes, 2014
High-throughput mass spectrometric (HT-MS) study is the method of choice for monitoring global changes in proteome. Data derived from these studies are meant for further validation and experimentation to discover novel biological insights.
Balakrishnan, Satish   +4 more
core   +2 more sources

Parsimony in Protein Conformational Change [PDF]

open access: yesStructure, 2015
Protein conformational change is analyzed by finding the minimalist backbone torsion angle rotations that superpose crystal structures within experimental error. Of several approaches for enforcing parsimony during flexible least-squares superposition, an ℓ(1)-norm restraint provided greatest consistency with independent indications of flexibility from
Jack J. Skalicky   +4 more
openaire   +3 more sources

Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ

open access: yesBiomolecules, 2020
How sequences of intrinsically disordered proteins (IDPs) code for their conformational dynamics is poorly understood. Here, we combined NMR spectroscopy, small-angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations to characterize the ...
Alan Hicks   +3 more
doaj   +1 more source

Reactive Human Plasma Glutathione Peroxidase Mutant with Diselenide Bond Succeeds in Tetramer Formation

open access: yesAntioxidants, 2022
Plasma glutathione peroxidase (GPx3) belongs to the GPx superfamily, and it is the only known secreted selenocysteine (Sec)−containing GPx in humans.
Zhenlin Fan   +3 more
doaj   +1 more source

Effectiveness of Riboflavin and Rose Bengal Photosensitizer Modified Adhesive Resin for Orthodontic Bonding

open access: yesPharmaceuticals, 2021
This study aimed to evaluate the effect of riboflavin (RF) and Rose Bengal (RB) photosensitizer modified adhesive resin on the degree of conversion (DC), and antimicrobial capacity after bonded to tooth surface. Different concentrations of RB and RF were
Ali Alqerban
doaj   +1 more source

Coupling of a Microfluidic Mixer to a Fourier-transform Infrared Spectrometer for Protein-Conformation Studies

open access: yesCHIMIA, 2011
The biological properties of a protein critically depend on its conformation, which can vary as a result of changes in conditions such as pH or following the addition of various substances.
Denis Prim   +2 more
doaj   +1 more source

Protein conformation in pure and hydrated deep eutectic solvents.

open access: yesPhysical Chemistry, Chemical Physics - PCCP, 2017
Deep eutectic solvents (DES) have recently been postulated as possible environments where protein structure may be preserved in the absence of water. Here we present our results towards understanding protein conformation in choline chloride-based DES and
A. Sanchez-Fernandez   +6 more
semanticscholar   +1 more source

Cycle-based formulations in Distance Geometry

open access: yesOpen Journal of Mathematical Optimization, 2023
The distance geometry problem asks to find a realization of a given simple edge-weighted graph in a Euclidean space of given dimension $K$, where the edges are realized as straight segments of lengths equal (or as close as possible) to the edge weights ...
Liberti, Leo   +3 more
doaj   +1 more source

Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Caenorhabditis elegans Lysates [PDF]

open access: yes, 2018
Protein aggregation is a hallmark of several neurodegenerative diseases and is associated with impaired protein homeostasis. This imbalance is caused by the loss of the protein's native conformation, which ultimately results in its aggregation or ...
Mata Cabana, Alejandro   +3 more
core   +2 more sources

Conformational transition of a myelin protein [PDF]

open access: yesFEBS Letters, 1971
An interesting transition from conformation to p-structure has been reported for phosvitin [ 1, 21. Taborsky [l] found that the transition from random to &structure was induced by low pH (1.8) and was reversed by raising the pH. Perlman and Grizzuti [2] found that at pH 2.0 phosvitin had a /3-structure, while in the pH range 6.0-10.0 the ORD and CD ...
John Anthony, Mario A. Moscarello
openaire   +3 more sources

Home - About - Disclaimer - Privacy