Michael T. Lerch

Unliganded Active State of the β2-Adrenergic Receptor Revealed by Pressure-Resolved DEER and ProGuide Molecular Modeling

This study reveals the unliganded active state of the β2-adrenergic receptor using pressure-resolved DEER and ProGuide modeling, showing pressure-dependent conformational changes and allosteric coupling.

The role of intrinsically disordered domains in regulating G protein coupled receptor signaling

This study uses single-molecule imaging to show how agonist-specific dynamics in structured and disordered regions of the 2AAR regulate signaling and function.

A biased allosteric modulator functions as a molecular glue to induce β2AR dimerization

The paper shows that AP-7-168 induces β2AR dimerization by acting as a molecular glue, revealing a new allosteric mechanism for GPCR modulation.

A High-Sensitivity Stopped-Flow EPR System to Monitor Millisecond Conformational Kinetics in Spin-Labeled Proteins

The paper develops a high-sensitivity stopped-flow EPR system for studying millisecond protein conformational dynamics, demonstrating its use on T4 lysozyme and β2 adrenergic receptor.

ProGuide: a flexible framework for modeling global conformational rearrangements in proteins using DEER-derived distance restraints

ProGuide generates structural models of protein conformations using DEER-derived distance restraints, revealing novel conformational states in the angiotensin II type 1 receptor.

Improved EPR sensitivity for aqueous biological samples using low-volume multi-channel cells and dielectric resonators

This paper improves EPR sensitivity for small aqueous biological samples using optimized dielectric resonators and multi-channel cells.

Structure and dynamics determine G protein coupling specificity at a class A GPCR

This study identifies structural features determining G protein coupling specificity at a class A GPCR using a Gi-biased agonist.

A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins

The paper introduces a pressure-jump EPR system to measure millisecond conformational exchange rates in spin-labeled proteins and demonstrates its application to T4 lysozyme.