Analysis of Quaternary Structure by Electron Microscope (CAT#: STEM-B-0381-CJ)

Introduction

Structure and conformation of a biological molecule is key for its function. The higher order structure of a biopharmaceutical molecule is, thereby, often directly connected to the quality, stability, safety, and efficacy of a therapy. The higher order structure is considered a critical quality attribute and, thus, a detailed understanding of the higher order structure of a biopharmaceutical compound is critical in every research and development phase. Characterizing the secondary, tertiary and, if present, quaternary structure of a biopharmaceutical compound requires multiple analytical techniques.

Many proteins are made up of more than one polypeptide chain to perform their function. The complete structure of such a protein is designated its quaternary structure, and each polypeptide chain is referred to as a subunit. The quaternary structure is stabilized by the same bonds as for the tertiary structure, including different noncovalent bonds and disulfide bonds. These bonds hold the subunits together and arrange themselves to form a larger protein complex.