Effect of Extrusion Parameters on Soybean Protein Conformation [PDF]
The study investigated the effect of different extrusion parameters: temperature, material moisture of raw material, and screw speed on the conformation of soybean protein.
ZHANG Haojia, ZHU Xiuqing, SUN Ying
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Parsimony in Protein Conformational Change [PDF]
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
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Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins [PDF]
Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a high level of structural heterogeneity and are best described by ensembles consisting of multiple conformations with associated thermodynamic weights.
arxiv
Structural interrogation of phosphoproteome identified by mass spectrometry reveals allowed and disallowed regions of phosphoconformation [PDF]
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
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Role of Pre-molten Globule Structure in Protein Amyloid Fibril Formation [PDF]
The conversion of a protein from its native conformation to the pathogenic form is a critical event in the pathogenesis of several neurodegenerative disorders such as Alzheimer’s (AD), Parkinson’s, and Huntington’s diseases, along with type II diabetic ...
Ali Es-haghi+2 more
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Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Caenorhabditis elegans Lysates [PDF]
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
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Conformational transition of a myelin protein [PDF]
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
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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
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Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ
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
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Conformational kinetics reveals affinities of protein conformational states [PDF]
Significance Despite 50 years of studies of coupled binding and conformational change reactions in proteins and nucleic acids, there has been no detailed analysis of the affinities of the multiple conformational states involved. The relationship between these affinities and the dynamics of conformational change has also been largely ...
Daniels, Kyle G+2 more
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