Now showing items 1-10 of 376
Prediction of Spontaneous Protein Deamidation from Sequence-Derived Secondary Structure and Intrinsic Disorder
(Public Library Of Science, 2015-12)
Asparagine residues in proteins undergo spontaneous deamidation, a post-translational modification that may act as a molecular clock for the regulation of protein function and turnover. Asparagine deamidation is modulated ...
Cold shock protein a from Corynebacterium pseudotuberculosis: Role of electrostatic forces in the stability of the secondary structure
The conformational stability of the Cold shock protein A (CspA) from C. pseudotuberculosis (Cp), a nucleic acid binding protein in function of pH and salt concentration was examined by using differential scanning calorimetry ...
Analysis of secondary structure in proteins by chemical cross-linking coupled to MS
alpha and beta Conformational preferences in fibril forming peptides characterised using NMR and CD techniques
(Ios PressAmsterdamHolanda, 2004)
Changes in secondary structure of gluten proteins due to emulsifiers
(Elsevier Science, 2013-02-06)
Changes in the secondary structure of gluten proteins due to emulsifiers were analyzed by Raman Spectroscopy. The protein folding induced by 0.25% SSL (Sodium Stearoyl Lactylate) (GS0.25, Gluten + 0.25% SSL) included an ...
Expression, purification and characterization of cold shock protein A of Corynebacterium pseudotuberculosis
(Elsevier B.V., 2015-08-01)
The gram-positive bacterium Corynebacterium pseudotuberculosis is the causative agent of different diseases that cause dramatically reduced yields of wool and milk, and results in weight loss, carcass condemnation and also ...
Mapping eIF5A binding sites for Dys1 and Lia1: In vivo evidence for regulation of eIF5A hypusination
The evolutionarily conserved factor eIF5A is the only protein known to undergo hypusination, a unique posttranslational modification triggered by deoxyhypusine synthase (Dys1). Although eIF5A is essential for cell viability, ...