Results 71 to 80 of about 3,930,063 (310)

CHAPTER 1.1. Disulfide Bonds in Protein Folding and Stability [PDF]

open access: yes, 2018
Disulfide bonds are unique among post-translational modifications, as they add covalent crosslinks to the polypeptide chain. Accordingly, they can exert pronounced effects on protein folding and stability. This is of particular importance for secreted or
Sub Cellular Protein Chemistry   +7 more
core   +1 more source

Defining essential charged residues in fibril formation of a lysosomal derived N-terminal α-synuclein truncation

open access: yesNature Communications
N- and C-terminal α-synuclein (α-syn) truncations are prevalent in Parkinson’s disease. Effects of the N- and C-terminal residues on α-syn aggregation and fibril propagation are distinct, where the N-terminus dictates fibril structure. Here, the majority
Ryan P. McGlinchey   +4 more
doaj   +1 more source

Effects of Aqueous Extract of Zanthoxylum bungeanum on Gel Properties of Mandarin Fish (Siniperca chuatsi) Surimi Gel

open access: yesShipin gongye ke-ji, 2023
In this study, the effect of Zanthoxylum bungeanum aqueous extract (ZBAE) with the addition of 0, 0.125%, 0.25%, 0.5% and 1.0% on the characteristics of mandarin fish surimi gel, including water-holding capacity, gel strength, texture, whiteness ...
Haiqiu WEI   +5 more
doaj   +1 more source

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 ...
Anthony, John, Moscarello, M.A.
openaire   +2 more sources

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

open access: yesFEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura   +2 more
wiley   +1 more source

Alteration of protein function by a silent polymorphism linked to tRNA abundance [PDF]

open access: yes, 2017
Synonymous single nucleotide polymorphisms (sSNPs) are considered neutral for protein function, as by definition they exchange only codons, not amino acids.
Sebastian Kirchner   +27 more
core   +2 more sources

Orthopaedic health, conformation and longevity in riding horses [PDF]

open access: yes, 2013
Soundness and longevity of the riding horse play a central role for animal welfare, sport performance and horse owner economy. Routine registration of health traits in horses is rare. Thus, knowledge of genetic variation in health of horses and long term
Jönsson, Lina
core   +1 more source

A model of protein conformational substates [PDF]

open access: yesProceedings of the National Academy of Sciences, 1985
Many proteins have been observed to exist in a large number of conformations that are believed to play an important role in their dynamics. A model of protein conformational substates that incorporates the ideas of frustration and disorder in analogy to glasses and spin glasses is proposed.
openaire   +2 more sources

Predicting conformational switches in proteins [PDF]

open access: yesProtein Science, 1999
AbstractWe describe a new computational technique to predict conformationally switching elements in proteins from their amino acid sequences. The method, called ASP (Ambivalent Structure Predictor), analyzes results from a secondary structure prediction algorithm to identify regions of conformational ambivalence. ASP identifies ambivalent regions in 16
M, Young   +3 more
openaire   +2 more sources

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

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