This Health Research Program opportunity is with Dr. Steven Chou, Molecular Biology & Biophysics.
Project Description: Biochemical Characterization of the NPR1 Transmembrane Signaling Complex.
Natriuretic peptide receptor 1 (NPR1) is a single-transmembrane guanylyl cyclase that plays a critical role in regulating blood pressure. The binding of atrial natriuretic peptide (ANP) to the extracellular domain (ECD) of NPR1 induces conformational changes in the transmembrane helices, propagating the signal to the intracellular domain (ICD) and its binding partners. However, the structural and biochemical characterization of NPR1 has been challenging due to its extensive post-translational modifications (PTMs) and high conformational flexibility, which hinder analysis using overexpression systems.
To overcome these challenges, we propose an alternative approach to isolate the NPR1 signaling complex directly from natural sources. We aim to purify the intact complex and identify its components using mass spectrometry.
For full details about this Health Research Program opportunity, visit https://ugradresearch.uconn.edu/hrpsu25-5
For full details about the Health Research Program, visit ugradresearch.uconn.edu/hrp/
Submissions to this program are made via a third-party software application, SurveyMonkey Apply. The terms of use and privacy statements for this software apply to your use of it and to the information you provide in your application. Before proceeding with your submission, please review their terms and privacy statements linked below.
HRP SU25-5: Research Opportunity with Dr. Steven Chou
This Health Research Program opportunity is with Dr. Steven Chou, Molecular Biology & Biophysics.
Project Description: Biochemical Characterization of the NPR1 Transmembrane Signaling Complex.
Natriuretic peptide receptor 1 (NPR1) is a single-transmembrane guanylyl cyclase that plays a critical role in regulating blood pressure. The binding of atrial natriuretic peptide (ANP) to the extracellular domain (ECD) of NPR1 induces conformational changes in the transmembrane helices, propagating the signal to the intracellular domain (ICD) and its binding partners. However, the structural and biochemical characterization of NPR1 has been challenging due to its extensive post-translational modifications (PTMs) and high conformational flexibility, which hinder analysis using overexpression systems.
To overcome these challenges, we propose an alternative approach to isolate the NPR1 signaling complex directly from natural sources. We aim to purify the intact complex and identify its components using mass spectrometry.
For full details about this Health Research Program opportunity, visit https://ugradresearch.uconn.edu/hrpsu25-5
For full details about the Health Research Program, visit ugradresearch.uconn.edu/hrp/
Submissions to this program are made via a third-party software application, SurveyMonkey Apply. The terms of use and privacy statements for this software apply to your use of it and to the information you provide in your application. Before proceeding with your submission, please review their terms and privacy statements linked below.