Research interests in our research group

NMR spectroscopy stands as a unique technique amongst all biophysical tools enabling studies of biomolecular structures at atomic resolution in solution while simultaneously providing also site-specific data on dynamics and molecular interactions that regulate life at the molecular level. Our group seeks to understand protein function through characterization of structure, dynamics and interactions in solution. We mainly focus on proteins and molecular systems whose structures or interactions are dynamic and transient i.e. systems that are difficult to study with the X-ray crystallography e.g., intrinsically disordered proteins (IDPs) and modular systems.

We boost our efforts in structural and functional studies of biomolecules by participating strongly in NMR method development. We aim to advance and disseminate routines which help to obtain more information with reduced time and effort. Novel strategies devised for assignment of IDPs, as well as optimized methods developed for measuring structural and dynamical information on larger proteins, have had key role in studies of several challenging molecular targets.

Our current research is focused on:
- Development of NMR methodology for structural and functional studies of biological molecules
- Intrinsically disordered proteins/systems
- Structural basis of pathogen - host interactions, especially bacterial and viral effectors targeting SH3 domains
- Structural and functional characterization of peptidoglycan hydrolysing M23 enzymes

Keywords: Alphavirus, EHEC/EPEC, IDPs, M23 peptidases, NMR spectroscopy, S. aureus, SH3 domains


Selected publications

Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family. Raulinaitis V, Tossavainen H, Aitio O, Juuti JT, Hiramatsu K, Kontinen V, Permi P. Sci Rep, 2017, 7:6020. [PUBMED]

Bridge over troubled proline: assignment of intrinsically disordered proteins using (HCA)CON(CAN)H and (HCA)N(CA)CO(N)H experiments concomitantly with HNCO and i(HCA)CO(CA)NH. Hellman M, Piirainen H, Jaakola VP, Permi P. J Biomol NMR, 2014, 58:49. [PUBMED]

Recognition of tandem PxxP motifs as a unique Src homology 3 -binding mode triggers pathogen-driven actin assembly. Aitio O, Hellman M, Kazlauskas A, Vingadassalom DF, Leong JM, Saksela K, Permi P. Proc Natl Acad Sci U.S.A., 2010, 107:21743. [PUBMED]