ScienceGuardians is the 1st fully verified journal club
Secure Environment: Verified contributors only, ensuring meaningful and responsible discussions. Members can stay anonymous while verified, ensuring legitimacy and accountability.
Combatting Misconduct: A fortress against anonymous intimidation and coordinated campaigns, fostering evidence-based dialogue and protecting the academic community.
Resources and Training: Access classified content, participate in enlightening debates, and stay at the forefront of ethical practices.
Hack-Proof Platform: Your privacy is paramount. The identity information of users choosing to remain anonymous is securely stored offline.
Our Commitment:
Integrity and Accountability: Every account verified for credible and responsible engagement.
Inclusivity and Fairness: A platform where all voices in the scientific community are respected.
Support and Collaboration: Helping resolve issues delicately and constructively.
Participant
Have the authors considered accounting for protein flexibility in their molecular docking simulations, particularly within the dynamic ATPase domains of p97? Since the D1 and D2 domains undergo significant conformational changes, rigid docking may not fully capture the inhibitors’ binding interactions. Would molecular dynamics simulations or induced-fit docking provide additional insights into binding stability?