Results 251 to 260 of about 295,099 (303)

Post‐Translational Isoaspartate Promotes Amyloid Formation in β2‐Microglobulin

open access: yesAngewandte Chemie, EarlyView.
Chemical synthesis of five β2‐microglobulin (β2m) variants reveals the structural impact of Asn deamidation. By introducing Asp or isoAsp at susceptible Asn‐Gly sequences, we demonstrate that isoAsp17 formation specifically accelerates amyloid fibril formation, highlighting its potential contribution to dialysis‐related amyloidosis.
Ryuji Kawakami   +5 more
wiley   +1 more source

Stability and Conformational Dynamics of Interferons: Structural Insights into the Urea- and Guanidinium Chloride-Induced Unfolding. [PDF]

open access: yesACS Omega
Aiman A   +10 more
europepmc   +1 more source

DENATURED STATES OF PROTEINS

Annual Review of Biochemistry, 1991
The denatured "state" of a protein is a distribution of many different molecular conformations, the averages of which are measured by experiments. The properties of this ensemble depend sensitively on the solution conditions. There is now considerable evidence that even in strong denaturants such as 6M GuHC1 and 9M urea, some structure may remain in ...
K A, Dill, D, Shortle
openaire   +2 more sources

Denaturation of Fish Proteins

Nature, 1957
REPORTING on the influence of freezing-rate on the denaturation of cold-stored fish, Love1 states that organoleptically determined toughness of cod, stored at − 30° C., does not always involve decreased protein solubility.
openaire   +3 more sources

Cold Denaturation of Protein

Critical Reviews in Biochemistry and Molecular Biology, 1990
This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride. The facts obtained by various experimental techniques are analyzed thermodynamically and it is shown that the cold denaturation is a ...
openaire   +2 more sources

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