Selected amyloid structures available in the Protein Data Bank have been subjected to a comparative analysis. Classification is based on the distribution of hydrophobicity in amyloids that differ with respect to sequence, chain length, the distribution of beta folds, protofibril structure, and the arrangement of protofibrils in each superfibril. The study set includes the following amyloids: $A\beta$ (1-42), which is listed as $A\beta$ (15-40) and carries the D23N mutation, and $A\beta$ (11-42) and $A\beta$ (1-40), both of which carry the $E22\Delta$ mutation, tau amyloid, and $\alpha$-synuclein. Based on the fuzzy oil drop model (FOD), we determined that, despite their conformational diversity, all presented amyloids adopt a similar...
A set of short peptide sequences susceptible to fibrillar aggregation produces sequneces capable of ...
In this paper we show that the fuzzy oil drop model represents a general framework for describing th...
Schematic presentation of loops (7 aa) linking two β-strands (fragments of β-sheets). The left one –...
Selected amyloid structures available in the Protein Data Bank have been subjected to a comparative...
Conceptual image showing the unrestricted capability for linear propagation of bands characterized b...
Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloi...
We propose a mathematical model describing the formation of micellar forms—whether spherical, globul...
The image depicts a highly regular, spherically symmetrical structure. Shades of gray correspond to ...
Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloi...
The existence of polypeptide chain fragments in which identical sequences translate into different s...
Protein structure is the result of the high synergy of all amino acids present in the protein. This...
AbstractAmyloid-β, the protein implicated in Alzheimer’s disease, along with a number of other prote...
Current interest in studying amyloid fibrils arises from their involvement in different fields (Chit...
AbstractAmyloid fibrillar aggregates of proteins or peptides are involved in the etiology of several...
The object of our analysis is the structure of alpha-synuclein (ASyn), which, under in vivo conditi...
A set of short peptide sequences susceptible to fibrillar aggregation produces sequneces capable of ...
In this paper we show that the fuzzy oil drop model represents a general framework for describing th...
Schematic presentation of loops (7 aa) linking two β-strands (fragments of β-sheets). The left one –...
Selected amyloid structures available in the Protein Data Bank have been subjected to a comparative...
Conceptual image showing the unrestricted capability for linear propagation of bands characterized b...
Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloi...
We propose a mathematical model describing the formation of micellar forms—whether spherical, globul...
The image depicts a highly regular, spherically symmetrical structure. Shades of gray correspond to ...
Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloi...
The existence of polypeptide chain fragments in which identical sequences translate into different s...
Protein structure is the result of the high synergy of all amino acids present in the protein. This...
AbstractAmyloid-β, the protein implicated in Alzheimer’s disease, along with a number of other prote...
Current interest in studying amyloid fibrils arises from their involvement in different fields (Chit...
AbstractAmyloid fibrillar aggregates of proteins or peptides are involved in the etiology of several...
The object of our analysis is the structure of alpha-synuclein (ASyn), which, under in vivo conditi...
A set of short peptide sequences susceptible to fibrillar aggregation produces sequneces capable of ...
In this paper we show that the fuzzy oil drop model represents a general framework for describing th...
Schematic presentation of loops (7 aa) linking two β-strands (fragments of β-sheets). The left one –...