Related Experiment Video
Updated: May 12, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Regulation of conjugated hemoglobin on micelles through copolymer chain sequences and the protein's isoelectric
1State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China.
Abstract:
Amphiphilic triblock copolymers with carbonyl groups located either in the middle segment or in the third side block are synthesized by adjusting feeding sequence of the comonomers. The conjugation of hemoglobin (Hb) on the copolymer micelles is realized by condensation reactions of carbonyl with the amino groups of Hb, and the gas-binding capacity of Hb is well preserved. Interestingly, the reassembly behavior of Hb-conjugated micelles (HbM) is explored by adjusting the pH. As for triblock copolymers with a carbonyl-functionalized segment as the third block, Hb is rearranged into the inner core of micelles when the pH is adjusted close to the isoelectric point of Hb. Therefore, it may provide a new needed route for fabrication of protein carriers, which is different from the traditional encapsulation technique.
Related Concept Videos
Micelles
Cooperative Allosteric Transitions
Conjugated Proteins
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Coagulation
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Extraction: Advanced Methods
