Agnes J.O. Jong

Nanyang Technological University

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Milton T. W. Hearn

Monash University

Reinhard I. Boysen

Monash University

Albert Guskov

University of Groningen

Terri Phua

Nanyang Technological University

Anna-Karin Lundbäck

Nanyang Technological University

Tobias Cornvik

Nanyang Technological University

Said Eshaghi

Nanyang Technological University

Nurhuda Nordin

Infrastructure University Kuala Lumpur

Helena Engman

AstraZeneca (United Kingdom)

Muralee Muraledaran

Cooperative Institutions

Karolinska Institutet

Nanyang Technological University

Centre National de la Recherche Scientifique

Stockholm University

Monash University

Australian Research Council

Australian Regenerative Medicine Institute

CSIRO Manufacturing

Monash Institute of Medical Research

Australian Centre for Research on Separation Science

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Binding behaviour and conformational properties of globular proteins in the presence of immobilised non-polar ligands used in reversed-phase liquid chromatography

Journal of Chromatography A (2005)

Reinhard I. Boysen Agnes J.O. Jong Milton T. W. Hearn

Globular protein

Hydrophobic effect

10.1016/j.chroma.2005.03.097

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Citations (15)

Thermodynamic Assessment of the Stability of Thrombin Receptor Antagonistic Peptides in Hydrophobic Environments

Biophysical Journal (2002)

Reinhard I. Boysen Agnes J.O. Jong Milton T. W. Hearn

In this paper, a general procedure is described to determine thermodynamic parameters associated with the interaction of thrombin receptor antagonistic peptides (TRAPs) with immobilized nonpolar ligands. The results show that these interactions were associated with nonlinear van't Hoff dependencies over a wide temperature range. Moreover, changes in relevant thermodynamic parameters, namely the changes in Gibbs free energy of interaction, ΔGassoc0, enthalpy of interaction, ΔHassoc0 entropy of interaction, ΔSassoc0, and heat capacity, ΔCp0, have been related to the structural properties of these TRAP analogs. The implications of these investigations for the design of thrombin receptor agonists/antagonists with structures stabilized by intramolecular hydrophobic interactions are discussed.

Hydrophobic effect

10.1016/s0006-3495(02)75574-4

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Citations (18)

On the binding behaviour and conformational properties of polypeptides and globular proteins with non-polar ligates

Milton T. W. Hearn Reinhard I. Boysen Muralee Muraledaran Agnes J.O. Jong

Globular protein

Source

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Citations (1)

Structural insights into substrate recognition in proton‐dependent oligopeptide transporters

EMBO Reports (2013)

Fatma Guettou E.M. Quistgaard L. Tresaugues Per Moberg Caroline Jegerschöld

Major facilitator superfamily

Oligopeptide

Subfamily

Shewanella oneidensis

Tetrapeptide

Peptidomimetic

10.1038/embor.2013.107

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Citations (102)

Role of Interfacial Hydrophobic Residues in the Stabilization of the Leucine Zipper Structures of the Transcription Factors c-Fos and c-Jun

Journal of Biological Chemistry (2002)

Reinhard I. Boysen Agnes J.O. Jong Matthew C. J. Wilce Glenn F. King Milton T. W. Hearn

This study documents a new and versatile experimental approach to study the relative stabilization energetics of recombinant polypeptide and protein mutants. In particular, the effect of temperature change over the range of T = 278–338 K on the thermodynamics of interaction of several leucine zipper coiled-coil polypeptides related to the transcription factors, c-Fos and c-Jun, following binding to immobilized n-octyl ligands has been determined. Plots of the change in heat capacity, ΔC p0, versus T, in combination with the corresponding van't Hoff plots, allow the energetics of the interaction of polypeptides withn-octyl ligands to be rationalized and the respective mid-point transition temperatures, T_m values, determined for the melting of their supramolecular structures. The derived experimental data correlated well with information available from other procedures, confirming that this new approach provides complementary insight into the interaction thermodynamics and the molecular nature of the thermal stability of recombinant polypeptides in non-polar or other types of chemical environments.

Zipper

Transcription

bZIP domain

ATF3

10.1074/jbc.m104556200

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Citations (42)

The complete structure of CorA magnesium transporter from Methanocaldococcus jannaschii

Albert Guskov Nurhuda Nordin A. Reynaud Helena Engman Anna-Karin Lundbäck

10.2210/pdb4ev6/pdb

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Structural insights into the mechanisms of Mg ²⁺ uptake, transport, and gating by CorA

Proceedings of the National Academy of Sciences (2012)

Albert Guskov Nurhuda Nordin A. Reynaud Henrik Engman Anna-Karin Lundbäck

Despite the importance of Mg 2+ for numerous cellular activities, the mechanisms underlying its import and homeostasis are poorly understood. The CorA family is ubiquitous and is primarily responsible for Mg 2+ transport. However, the key questions—such as, the ion selectivity, the transport pathway, and the gating mechanism—have remained unanswered for this protein family. We present a 3.2 Å resolution structure of the archaeal CorA from Methanocaldococcus jannaschii , which is a unique complete structure of a CorA protein and reveals the organization of the selectivity filter, which is composed of the signature motif of this family. The structure reveals that polar residues facing the channel coordinate a partially hydrated Mg 2+ during the transport. Based on these findings, we propose a unique gating mechanism involving a helical turn upon the binding of Mg 2+ to the regulatory intracellular binding sites, and thus converting a polar ion passage into a narrow hydrophobic pore. Because the amino acids involved in the uptake, transport, and gating are all conserved within the entire CorA family, we believe this mechanism is general for the whole family including the eukaryotic homologs.

Transport protein

Protein family

10.1073/pnas.1210076109

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Citations (77)

Thermodynamic analysis of the interaction of α-helical polypeptides and proteins with nonpolar ligands in reversed-phase HPLC

Agnes J.O. Jong

10.26180/14967660.v1

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Citations (0)

On the binding behaviour and conformational properties of Polypeptides and gobular proteins in hydrophobic environments

Milton T. W. Hearn Reinhard I. Boysen Muralee Muraledaran Agnes J.O. Jong