Results 61 to 70 of about 160,241 (252)
Aggregate Geometry in Amyloid Fibril Nucleation [PDF]
Physical Review Letters, 2013 We present and study a minimal structure-based model for the self-assembly of peptides into ordered beta-sheet-rich fibrils. The peptides are represented by unit-length sticks on a cubic lattice and interact by hydrogen bonding and hydrophobicity forces.
Irbäck, Anders +4 more
openaire +3 more sources
Formation and properties of whey protein fibrils [PDF]
, 2011 Protein fibrils are threadlike aggregates that are about one molecule thick and more than thousand molecules long. Due to their threadlike structure they could potentially be used to form meat-like structures.
Kroes-Nijboer, A.
core
Adenosine triphosphate as a modulator of protein interactions and stability
FEBS Open Bio, EarlyView.ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source
PLoS ONE, 2015 BackgroundSemen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection.
Jinquan Chen +9 more
doaj +1 more source
Advanced Functional Materials, EarlyView.Phase transitions are central for the assembly of recombinant silk proteins into fibers. Soluble protein can transition into condensed states such as condensates and gels. These states are metastable and evolve in a time‐dependent way. Metastability depends on the protein sequence, and this relationship can be used to enhance the mechanical properties ...
Fred‐Eric Sammalisto +5 more
wiley +1 more source
PLoS ONE, 2014 Formation of amyloid fibrils in vivo has been linked to disorders such as Alzheimer's disease and prion-associated transmissible spongiform encephalopathies.
Weronika Surmacz-Chwedoruk +4 more
doaj +1 more source
Trypsin Induced Degradation of Amyloid Fibrils
, 2021 Proteolytic enzymes are known to be involved in the formation and degradation of various monomeric proteins, but the effect of proteases on the ordered protein aggregates, amyloid fibrils, which are considered to be extremely stable, remains poorly ...
Irina Kuznetsova +6 more
core +1 more source
Beyond Primary Nucleation: Molecular Basis of Peptide Crystal Secondary Nucleation at Soft Interface
Advanced Functional Materials, EarlyView.High spatiotemporal‐resolution atomic force microscopy directly resolved peptide secondary nucleation (SN) and growth characteristics and mechanisms on HOPG. The landscape of peptide nucleation sites, growth dynamics, molecular‐scale structures, phase transitions, and cross‐seeding processes were realized.
Linhao Sun +2 more
wiley +1 more source
Communications Biology, 2021 Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable
Phuong Trang Nguyen +5 more
doaj +1 more source
Thermodynamics of β-amyloid fibril formation [PDF]
The Journal of Chemical Physics, 2004 Amyloid fibers are aggregates of proteins. They are built out of a peptide called β-amyloid (Aβ) containing between 41 and 43 residues, produced by the action of an enzyme which cleaves a much larger protein known as the amyloid precursor protein (APP).
G. Tiana +3 more
openaire +5 more sources