Academic Profile : Faculty
Assoc Prof Jaume Torres
Associate Professor, School of Biological Sciences
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Date of joining NTU: November 2001
Associate Professor
BSc, MSc and PhD, Universitat Autònoma de Barcelona (Catalonia, Spain)
Office: 04s-32
Telephone: 6316 2857
Email: jtorres@ntu.edu.sg
Professional Experience
Postdoctoral. University of Essex, UK
Postdoctoral. University of Cambridge,UK
Associate Professor
BSc, MSc and PhD, Universitat Autònoma de Barcelona (Catalonia, Spain)
Office: 04s-32
Telephone: 6316 2857
Email: jtorres@ntu.edu.sg
Professional Experience
Postdoctoral. University of Essex, UK
Postdoctoral. University of Cambridge,UK
Our work is focused on structural and functional aspects of membrane proteins, leading to understanding of their function and to development of drugs that will modify their activity.
One type of protein we explore is the aquaporins, the 'water channels' of the cell. Aquaporins selectively transport water and this makes them very useful for biotechnological applications such as water purification. In a medical context, aquaporins are found in most human cells and are involved in a vast array of pathological conditions, but no drugs are available for inhibition or activation. Therefore discovery of aquaporin inhibitors is one of our main interests.
Another system we study are small membrane proteins from enveloped viruses, which tend to oligomerize and form channels of different selectivities. Some examples are M2 from influenza A virus, p7 from hepatitis C virus, SH from respiratory syncytial virus and coronavirus envelope proteins. No structural data exists for the full length version of these proteins despite their small size (typically less than 100 amino acids). Further, their flexibility likely contributes to their multiple reported functions.
One type of protein we explore is the aquaporins, the 'water channels' of the cell. Aquaporins selectively transport water and this makes them very useful for biotechnological applications such as water purification. In a medical context, aquaporins are found in most human cells and are involved in a vast array of pathological conditions, but no drugs are available for inhibition or activation. Therefore discovery of aquaporin inhibitors is one of our main interests.
Another system we study are small membrane proteins from enveloped viruses, which tend to oligomerize and form channels of different selectivities. Some examples are M2 from influenza A virus, p7 from hepatitis C virus, SH from respiratory syncytial virus and coronavirus envelope proteins. No structural data exists for the full length version of these proteins despite their small size (typically less than 100 amino acids). Further, their flexibility likely contributes to their multiple reported functions.
- Activation Mechanism of A Protein Water Channel by Cardiolipin: Implications for the Fabrication of Block Copolymer Nanosheets
- Biophysical characterization of membrane proteins
- Structural variation and inhibition of key coronaviral ion channels
US 2014/0332468 A1: Aquaporin Based Thin Film Composite Membranes (2024)
Abstract: Present invention relates to a thin film composite membrane wherein a thin selective layer, having incorporated amphiphilic vesicles, is supported by a microporous substrate. A process of preparing the thin film composite membrane and its use are also disclosed.
Abstract: Present invention relates to a thin film composite membrane wherein a thin selective layer, having incorporated amphiphilic vesicles, is supported by a microporous substrate. A process of preparing the thin film composite membrane and its use are also disclosed.