Results 91 to 100 of about 6,845,089 (390)
This work presents the characterization of MvoDUF2193, a Methanococcus voltae (Mvo) protein from the domain of unknown function (DUF) 2193 family. We demonstrate that MvoDUF2193 binds a single [4Fe–4S] cluster per subunit and that cluster occupancy regulates the transition from an apo tetramer to a [4Fe–4S] monomeric form. This structural transition is
Emily M. Dieter+8 more
wiley +1 more source
The importance of protein folding in the biosynthesis of proteins is reviewed.
openaire +2 more sources
Prion diseases are fatal transmissible neurodegenerative diseases that affect many mammals, including humans, caused by the templated misfolding of the prion protein.
Hailey Pineau, Valerie L. Sim
doaj +1 more source
An ancient conserved role for prion protein in learning and memory
The misfolding of cellular prion protein (PrPC) to form PrP Scrapie (PrPSc) is an exemplar of toxic gain-of-function mechanisms inducing propagated protein misfolding and progressive devastating neurodegeneration. Despite this, PrPC function in the brain
Patricia L. A. Leighton+4 more
doaj +1 more source
Quality control of protein reagents for the improvement of research data reproducibility
Proteins and peptides are amongst the most widely used research reagents but often their quality is inadequate and can result in poor data reproducibility. Here we propose a simple set of guidelines that, when correctly applied to protein reagents should
Ario de Marco+10 more
doaj +1 more source
Periodic force induced stabilization or destabilization of the denatured state of a protein
We have studied the effects of an external sinusoidal force in protein folding kinetics. The externally applied force field acts on the each amino acid residues of polypeptide chains.
Bidhan Chandra Bag+4 more
core +1 more source
Functional role and folding properties of the glucan‐binding domain of oral bacterial glucansucrase
The role of the glucan‐binding domain in Streptococcus sobrinus glucansucrase was examined, focusing on its impact on enzymatic activity, dextran binding, and structural stability of deletion mutants and a circularly permuted protein. Our research revealed that glucosyl transfer efficiency is linked to cooperative interdomain folding.
Hideyuki Komatsu+5 more
wiley +1 more source
Influence of C-terminal truncation of murine Serum amyloid A on fibril structure
Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is the acute-phase reactant serum amyloid A (SAA) 1.1, the deposited fibrils consist mainly of C ...
Matthies Rennegarbe+4 more
doaj +1 more source
The yeast mitoribosome assembly factor Rsm22 contains a [4Fe‐4S] cluster that is matured by the mitochondrial iron–sulfur cluster assembly (ISC) machinery. Defects in ISC components result in impaired mitochondrial protein synthesis due to a mitoribosome assembly defect.
Ulrich Mühlenhoff+4 more
wiley +1 more source
Evidence suggests that beta-amyloid (Aβ)-induced phosphorylation/aggregation of tau protein plays a critical role in the degeneration of neurons and development of Alzheimer’s disease (AD), the most common cause of dementia affecting the elderly ...
Pallabi Sil Paul+9 more
doaj +1 more source