Biophysical Application of Calorimetric Methods to Protein Misfolding and Aggregation Examinations
White Paper Jul 04, 2017
Unfolded proteins fold into thermodynamically-favorable native structures under the correct physiological conditions for gain of function (Figure 1) [1-4]. The burial of hydrophobic regions in a protein's interior, along with the exposure of hydrophilic residues to aqueous solutions stabilizes native structures and ensures solubility. Active native proteins perform their biological functions through highly regulated intermolecular interactions with their binding partners, under thermodynamic control.
Related White Papers
Meeting Modern Data Integrity and Compliance RequirementsWhite Paper
The accuracy and completeness of data is crucial for safe product development and to prevent serious implications regarding human health.READ MORE
How to Identify Low-Abundance Modified Peptides with Proteomics Mass SpectrometryWhite Paper
We present a new simplicity-focused analytics methodology, called Sorcerer Score™ that allows low-abundance, modified peptides (LAMPs) to be rigorously identified within a hypothesis-driven framework based on high-accuracy precursor and fragment mass data. Accurate peptide ID is fundamental to accurate protein quantitation and post-translational modification (PTM) analysis.READ MORE
Big Data Lipidomics for Lipid Biomarker Identification and Drug DiscoveryWhite Paper
Data analysis process aiming at the identification of lipid biomarkers and the
evaluations of their performance.