Photo of Marielle Walti(mwalti)

Marielle Walti

Member of the Graduate Faculty,
Assistant Professor, Chemistry and Biochemistry-Sci,

Chemistry & Biochemistry - Sci
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Grant: $249.0K
How drugs work, how they target proteins, and how humans can intervene to modulate the underlying biological processes, has always intrigued me. This is why I enrolled to study pharmaceutical science at ETH Zürich (Switzerland), one of the premier research institutions in the world. I found that I was fascinated with the early phase of drug discovery and development, particularly using structure-based drug design. I therefore joined Dr. Emil Pai’s lab at the University Health Network in Toronto (Canada) for an internship, where I was working on fluoroacetate dehalogenases and learned how to use X-ray crystallography. For my Ph.D., I decided to join the group of Prof. Roland Riek in the Department of Chemistry and Applied Biosciences at ETH to become an expert in NMR spectroscopy. There, I successfully solved the Aβ42 fibril structure, which is the main component in plaques found in Alzheimer’s patients. After obtaining my Ph.D., I felt the desire to find new ways of how to interfere with protein aggregation, which if successful is an important route to slow the progression of Alzheimer’s and similar diseases. Thus, I became intrigued with using chaperones to control amyloidogenic diseases, just as nature does. I joined Dr. Marius Clore’s lab at NIH (Bethesda, MD, USA) to expand my knowledge of basic NMR methodologies with one of the world’s experts and to focus on those methodologies geared towards the study of sparsely populated intermediate states which play an outsized role in the aggregation processes.
Marielle Walti experts in nmr spectroscopy, structural biology, biochemistry, molecular biology, bioinformatics, biophysics, computational biology, biomaterials, tissue engineering, computational fluid dynamics, turbulence, protein structure prediction, molecular pharmacology, microbiology, astronomy, astrophysics, atomic force microscopy, supramolecular chemistry, regenerative medicine, drug delivery, genomics, cryo-electron microscopy, enzymology
Biological Structure 2 
Proteins and Enzymes 
Recent Grants
Logo of Towards the Understanding of How Chaperones Function and Prevent Amyloidogenic Diseases funding agency
2023 $249.0KActive
Towards the Understanding of How Chaperones Function and Prevent Amyloidogenic Diseases
Publications (28)
2022Defluorination Capability of l‐2‐Haloacid Dehalogenases in the HAD‐Like Hydrolase Superfamily Correlates with Active Site Compactness 
2022An Efficient Method of Expression and Purification of Amyloid-Beta (Aβ1–42) Peptide from E. coli 
2022Elucidation of a nutlin-derivative—HDM2 complex structure at the interaction site by NMR molecular replacement: A straightforward derivation 
2021Visualization of sparsely-populated lower-order oligomeric states of human mitochondrial Hsp60 by cryo-electron microscopy 
2021A weakened interface in the P182L variant of HSP27 associated with severe Charcot‐Marie‐Tooth neuropathy causes aberrant binding to interacting proteins 
2021Probing the Interaction of Huntingtin Exon‐1 Polypeptides with the Chaperonin Nanomachine GroEL 
2020The three-dimensional structure of human β-endorphin amyloid fibrils 
2019Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds 
2019Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27 
2018The NMR2 Method to Determine Rapidly the Structure of the Binding Pocket of a Protein–Ligand Complex with High Accuracy 
2018Probing the mechanism of inhibition of amyloid-β (1–42)–induced neurotoxicity by the chaperonin GroEL 
2018Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies 
2018Extensive sampling of the cavity of the GroEL nanomachine by protein substrates probed by paramagnetic relaxation enhancement 
2017Assignment and atomic-resolution structure of an A beta (1-42) amyloid fibril 
2017Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ (1-42) amyloid polymorph 
2017Binding of polythiophenes to amyloids: Structural mapping of the pharmacophore 
2017Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein 
2017Fast NMR‐Based Determination of the 3D Structure of the Binding Site of Protein–Ligand Complexes with Weak Affinity Binders 
2016NMR-based determination of the 3D structure of the ligand–protein interaction site without protein resonance assignment 
2016Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q‐Band DEER EPR Spectroscopy 
2016Atomic-resolution structure of a disease-relevant Aβ (1–42) amyloid fibril 
2016Solid-state NMR sequential assignment of an Amyloid-β (1–42) fibril polymorph 
2015Solution NMR Studies of Recombinant Aβ (1–42): From the Presence of a Micellar Entity to Residual β‐Sheet Structure in the Soluble Species 
2014Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability 
2014Protein aggregation in bacteria: functional and structural properties of inclusion bodies in bacterial cells 
2014Liquid-and Solid-State NMR Studies on the Alzheimer's Peptide and Method Development for Structure-Based Drug Design on an Oncoprotein 
2014Towards a true protein movie: a perspective on the potential impact of the ensemble-based structure determination using exact NOEs 
2014Residue‐Specific Structural Studies of Inclusion Bodies