Heat capacity studies of LZ-GCN4 by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0483-WXH)

Introduction

Gcn4 is a transcription factor and a “master regulator” for gene expression which regulates close to one tenth of the yeast genome.
A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. Leucine zippers are a dimerization motif of the bZIP (Basic-region leucine zipper) class of eukaryotic transcription factors. Leucine zippers are present in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes. They can also be annotated simply as ZIPs, and ZIP-like motifs have been found in proteins other than transcription factors and are thought to be one of the general protein modules for protein–protein interactions.
The energetics of formation of specific protein complexes with other proteins or nucleic acids is now attracting increasing attention since it actually represents a most basic biological function. The heat capacity plays a major role in the determination of the energetics of protein folding and molecular recognition. As such, a better understanding of this thermodynamic parameter and its structural origin will provide new insights for the development of better molecular design strategies.