Dr. Reid Alderson

Research Group Leader

Dr. Reid Alderson

Academic Career and Research Areas

Reid Alderson is driven by a fundamental interest in uncovering the molecular principles that govern protein structure, dynamics, and interactions. His research focuses on how proteins explore dynamic conformational ensembles and how these motions regulate biological function, particularly under conditions of cellular stress. In particular, he seeks to understand how spatiotemporal changes in the cellular environment enable molecular chaperones and proteolytic enzymes to recognize, stabilize, and remodel client proteins, and how these processes interface with protein degradation pathways to regulate protein turnover under normal and stress conditions.

Reid is particularly focused on developing and applying advanced NMR spectroscopy methods to characterize protein dynamics at atomic resolution. His research integrates measurements of structural propensities and conformational interconversion to link molecular motions with functional outcomes. By combining experimental and computational approaches, he aims to establish general principles that govern how protein dynamics contribute to stability, interaction specificity, and adaptive responses to stress.

Reid obtained his DPhil in structural biology and NMR spectroscopy from the University of Oxford in 2019. Much of his thesis was completed at the National Institutes of Health with Ad Bax. Reid was awarded prizes from the Nuffield Department of Medicine at Oxford and the Ampere Society for his PhD thesis. Subsequently, Reid was awarded Banting and CIHR Fellowships from the Canadian Institutes of Health Research to work with Lewis Kay at the University of Toronto. In 2024, he established his independent research group at the Helmholtz Center Munich, through a Helmholtz Investigator Grant, where he leads efforts to investigate the structural and dynamical basis of protein function in complex biological environments.

Fields of Work and Expertise

Structural Biology Biochemistry Biophysics Computational Biology Intrinsically disordered proteins NMR spectroscopy AlphaFold2 Molecular chaperones Proteolytic enzymes 

Professional Background

2010-2014

BSc

University of Wisconsin-Madison, USA

Supervisor: Prof. John L. Markley at the NMRFAM

2014-2019

PhD

University of Oxford, UK

Supervisors:  Prof. Justin L. P. Benesch, Prof. Andrew J. Baldwin

National Institutes of Health, USA 

Supervisor:  Dr. Adriaan Bax, FRS

2019-2022

Banting Postdoctoral Fellow

University of Toronto, Canada

Department of Biochemistry

Supervisor:  Prof. Lewis E. Kay, FRS

Since 2024

Group Leader at Helmholtz Munich

Helmholtz Investigator Grant

Molecular Targets and Therapeutics Center

Publications

2024 bioRxiv

I. Pritišanac*, T.R. Alderson§, Đ. Kolarić§, T. Zarin, S. Xie, A.X. Lu, A. Alam, A. Maqsdood, J.-Y. Youn, J.D. Forman-Kay*, A.M. Moses*

A functional map of the human intrinsically disordered proteome
2023 Proc. Natl. Acad. Sci.

T.R. Alderson§, I. Pritišanac§, Đ. Kolarić, A.M. Moses, J.D. Forman-Kay*

Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
2023 Proc. Natl. Acad. Sci.

A.I.M. Sever§, T.R. Alderson§*, E. Rennella*, J.A. Aramini, Z.H. Liu, R.W. Harkness, L.E. Kay*

Activation of caspase-9 on the apoptosome as studied by methyl-TROSY NMR
2021 EMBO J.

T.R. Alderson§, E. Adriaenssens§, R. Asselbergh, I. Pritišanac, H.Y. Gastall, M.A. Wälti, J.M. Louis, V. Timmerman*, A.J. Baldwin*, J.L.P. Benesch*

A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins
2019 Nat. Commun.

T.R. Alderson, J. Roche, H.Y. Gastall, D.M.D. Dias, I. Pritišanac, A. Bax, J.L.P. Benesch*, A.J. Baldwin*

Local unfolding of the HSP27 monomer regulates chaperone activity

Networks and Affiliations

Technical University of Munich

Technical University of Munich

Read more