Temperature-Dependent Hydrogen-Bond Geometry in Liquid Water (2007)
Kristofer Modig, Bernd G. Pfrommer, Bertil Halle
We have determined the hydrogen-bond geometry in liquid water from 0 to 80 °C by combining measurements of the proton magnetic shielding tensor with ab initio density functional calculations. The...
Denisov, Vladimir P, Peters, Jörg, Hörlein, Hans Dietrich, Halle, Bertil
Abstract is not available
Protein self-association in solution: The bovine {beta} -lactoglobulin dimer and octamer (2003)
Gottschalk, Michael, Nilsson, Hanna, Roos, Helena, Halle, Bertil
We have used proton magnetic relaxation dispersion (MRD) to study the self-association of bovine β-lactoglobulin variant A (BLG-A) as a function of temperature at pH 4.7 (dimer–octamer...
Water and urea interactions with the native and unfolded forms of a {beta}-barrel protein (2003)
Modig, Kristofer, Kurian, Elizabeth, Prendergast, Franklyn G., Halle, Bertil
A fundamental understanding of protein stability and the mechanism of denaturant action must ultimately rest on detailed knowledge about the structure, solvation, and energetics of the denatured...
Flexibility and packing in proteins. (2002)
Structural flexibility is an essential attribute, without which few proteins could carry out their biological functions. Much information about protein flexibility has come from x-ray...
Membrane flexibility in a dilute lamellar phase : a multinuclear magnetic resonance study (1994)
We demonstrate that the bending rigidity, κ, of amphiphilic bilayers can be accurately determined from the quadrupole splitting in the NMR spectrum. We study the lamellar phase in the system...
Membrane flexibility in a dilute lamellar phase : a multinuclear magnetic resonance study (1994)
We demonstrate that the bending rigidity, κ, of amphiphilic bilayers can be accurately determined from the quadrupole splitting in the NMR spectrum. We study the lamellar phase in the system...
Membrane flexibility in a dilute lamellar phase : a multinuclear magnetic resonance study (1994)
We demonstrate that the bending rigidity, κ, of amphiphilic bilayers can be accurately determined from the quadrupole splitting in the NMR spectrum. We study the lamellar phase in the system...
The shape of ionic micelles (1988)
Halle, Bertil, Landgren, Mikael, Jönsson, Bengt
Shape polydispersity and shape fluctuations in ionic surfactant micelles are analysed theoretically on the basis of a model for the free energy of deformation, incorporating interfacial and...
The shape of ionic micelles (1988)
Halle, Bertil, Landgren, Mikael, Jönsson, Bengt
Shape polydispersity and shape fluctuations in ionic surfactant micelles are analysed theoretically on the basis of a model for the free energy of deformation, incorporating interfacial and...
The shape of ionic micelles (1988)
Halle, Bertil, Landgren, Mikael, Jönsson, Bengt
Shape polydispersity and shape fluctuations in ionic surfactant micelles are analysed theoretically on the basis of a model for the free energy of deformation, incorporating interfacial and...
Sequence-specific binding of counterions to B-DNA
Denisov, Vladimir P., Halle, Bertil
Recent studies by x-ray crystallography, NMR, and molecular simulations have suggested that monovalent counterions can penetrate deeply into the minor groove of B form DNA. Such groove-bound ions...
Flexibility and packing in proteins
Structural flexibility is an essential attribute, without which few proteins could carry out their biological functions. Much information about protein flexibility has come from x-ray...
Biomolecular hydration: From water dynamics to hydrodynamics
Halle, Bertil, Davidovic, Monika
Thermally driven rotational and translational diffusion of proteins and other biomolecules is governed by frictional coupling to their solvent environment. Prediction of this coupling from...
Biomolecular cryocrystallography: Structural changes during flash-cooling
To minimize radiation damage, crystal structures of biological macromolecules are usually determined after rapid cooling to cryogenic temperatures, some 150–200 K below the normal physiological...
Molecular origin of time-dependent fluorescence shifts in proteins
Nilsson, Lennart, Halle, Bertil
Time-resolved fluorescence spectroscopy is used increasingly to probe molecular motions at the aqueous interfaces of biological macromolecules and membranes. By recording the time variation of the...
Protein Self-Association in Solution: The Bovine Pancreatic Trypsin Inhibitor Decamer
Gottschalk, Michael, Venu, Kandadai, Halle, Bertil
We have used magnetic relaxation dispersion to study bovine pancreatic trypsin inhibitor (BPTI) self-association as a function of pH, salt type and concentration, and temperature. The magnetic...
Stabilization of Internal Charges in a Protein: Water Penetration or Conformational Change?
Denisov, Vladimir P., Schlessman, Jamie L., Halle, Bertil
The ionizable amino acid side chains of proteins are usually located at the surface. However, in some proteins an ionizable group is embedded in an apolar internal region. Such buried ionizable...
In the presence of high concentrations of inert macromolecules, the self-association of proteins is strongly enhanced through an entropic, excluded-volume effect variously called macromolecular...
Sequence-specific binding of counterions to B-DNA
Denisov, Vladimir P., Halle, Bertil
Recent studies by x-ray crystallography, NMR, and molecular simulations have suggested that monovalent counterions can penetrate deeply into the minor groove of B form DNA. Such groove-bound ions...
Flexibility and packing in proteins
Structural flexibility is an essential attribute, without which few proteins could carry out their biological functions. Much information about protein flexibility has come from x-ray...
Biomolecular hydration: From water dynamics to hydrodynamics
Halle, Bertil, Davidovic, Monika
Thermally driven rotational and translational diffusion of proteins and other biomolecules is governed by frictional coupling to their solvent environment. Prediction of this coupling from...
Biomolecular cryocrystallography: Structural changes during flash-cooling
To minimize radiation damage, crystal structures of biological macromolecules are usually determined after rapid cooling to cryogenic temperatures, some 150–200 K below the normal physiological...
Molecular origin of time-dependent fluorescence shifts in proteins
Nilsson, Lennart, Halle, Bertil
Time-resolved fluorescence spectroscopy is used increasingly to probe molecular motions at the aqueous interfaces of biological macromolecules and membranes. By recording the time variation of the...
Protein Self-Association in Solution: The Bovine Pancreatic Trypsin Inhibitor Decamer
Gottschalk, Michael, Venu, Kandadai, Halle, Bertil
We have used magnetic relaxation dispersion to study bovine pancreatic trypsin inhibitor (BPTI) self-association as a function of pH, salt type and concentration, and temperature. The magnetic...
Stabilization of Internal Charges in a Protein: Water Penetration or Conformational Change?
Denisov, Vladimir P., Schlessman, Jamie L., Halle, Bertil
The ionizable amino acid side chains of proteins are usually located at the surface. However, in some proteins an ionizable group is embedded in an apolar internal region. Such buried ionizable...
In the presence of high concentrations of inert macromolecules, the self-association of proteins is strongly enhanced through an entropic, excluded-volume effect variously called macromolecular...
Protein hydration dynamics in solution: a critical survey.
The properties of water in biological systems have been studied for well over a century by a wide range of physical techniques, but progress has been slow and erratic. Protein hydration--the...
Protein self-association in solution: The bovine β -lactoglobulin dimer and octamer
Gottschalk, Michael, Nilsson, Hanna, Roos, Helena, Halle, Bertil
We have used proton magnetic relaxation dispersion (MRD) to study the self-association of bovine β-lactoglobulin variant A (BLG-A) as a function of temperature at pH 4.7 (dimer–octamer...
Water and urea interactions with the native and unfolded forms of a β-barrel protein
Modig, Kristofer, Kurian, Elizabeth, Prendergast, Franklyn G., Halle, Bertil
A fundamental understanding of protein stability and the mechanism of denaturant action must ultimately rest on detailed knowledge about the structure, solvation, and energetics of the denatured...
A dry ligand-binding cavity in a solvated protein
Qvist, Johan, Davidovic, Monika, Hamelberg, Donald, Halle, Bertil
Ligands usually bind to proteins by displacing water from the binding site. The affinity and kinetics of binding therefore depend on the hydration characteristics of the site. Here, we show that the...
Cell water dynamics on multiple time scales
Water–biomolecule interactions have been extensively studied in dilute solutions, crystals, and rehydrated powders, but none of these model systems may capture the behavior of water in the highly...
Dynamics at the Protein-Water Interface from 17O Spin Relaxation in Deeply Supercooled Solutions
Mattea, Carlos, Qvist, Johan, Halle, Bertil
Most of the decisive molecular events in biology take place at the protein-water interface. The dynamical properties of the hydration layer are therefore of fundamental importance. To characterize...