What is he best known for?
The fields of study he is best known for:
Gary J. Pielak mainly investigates Biochemistry, Macromolecular crowding, Globular protein, Biophysics and Crystallography.
Gary J. Pielak combines subjects such as Chemical physics, Conformational change and Signal transduction with his study of Macromolecular crowding.
Gary J. Pielak has included themes like Solvation, Cytoplasm, Compressibility and Physical chemistry in his Globular protein study.
His Biophysics study combines topics in areas such as Hydrogen bond, Polymer and Cytosol.
His work deals with themes such as Crowding and Protein stability, which intersect with Crystallography.
The study incorporates disciplines such as Stereochemistry and Site-directed mutagenesis in addition to Cytochrome c.
His most cited work include:
- FlgM gains structure in living cells (263 citations)
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). (253 citations)
- Impact of protein denaturants and stabilizers on water structure. (243 citations)
What are the main themes of his work throughout his whole career to date?
Gary J. Pielak mainly focuses on Biophysics, Biochemistry, Cytochrome c, Crystallography and Protein structure.
His Biophysics study incorporates themes from Cytoplasm, Macromolecular crowding, Protein stability, Function and Intracellular.
He works mostly in the field of Macromolecular crowding, limiting it down to topics relating to Globular protein and, in certain cases, Rotational diffusion, as a part of the same area of interest.
His Cytochrome c research includes elements of Hemeprotein, Heme, Stereochemistry and Electron transfer.
His Crystallography research is multidisciplinary, incorporating perspectives in Steric effects, Molecule, Denaturation and Protein folding.
His Protein structure study integrates concerns from other disciplines, such as Conformational change, Nuclear magnetic resonance spectroscopy, Protein secondary structure and Circular dichroism.
He most often published in these fields:
- Biophysics (27.94%)
- Biochemistry (26.47%)
- Cytochrome c (22.06%)
What were the highlights of his more recent work (between 2016-2021)?
- Biophysics (27.94%)
- Macromolecule (14.22%)
- Biochemistry (26.47%)
In recent papers he was focusing on the following fields of study:
Gary J. Pielak mostly deals with Biophysics, Macromolecule, Biochemistry, Desiccation and Intrinsically disordered proteins.
Gary J. Pielak has researched Biophysics in several fields, including Crystallography, Globular protein, Function, Nuclear magnetic resonance spectroscopy and Protein–protein interaction.
His work carried out in the field of Globular protein brings together such families of science as Circular dichroism and Protein folding.
The various areas that Gary J. Pielak examines in his Function study include Protein structure, Folding and Microscopy.
His Macromolecular crowding study in the realm of Macromolecule interacts with subjects such as SH3 domain.
His study involves Enzyme, Osmolyte and Cytoplasm, a branch of Biochemistry.
Between 2016 and 2021, his most popular works were:
- Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation (138 citations)
- A cell is more than the sum of its (dilute) parts: A brief history of quinary structure. (60 citations)
- Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine. (49 citations)
In his most recent research, the most cited papers focused on:
His primary scientific interests are in Biophysics, Macromolecule, Globular protein, Protein–protein interaction and Intrinsically disordered proteins.
His Biophysics research integrates issues from Dimer, Nuclear magnetic resonance spectroscopy, Molecule, Bovine serum albumin and Protein structure.
His Protein structure research incorporates themes from Compartmentalization, Protein stability and Function.
Specifically, his work in Macromolecule is concerned with the study of Macromolecular crowding.
His Globular protein study improves the overall literature in Crystallography.
The concepts of his Crystallography study are interwoven with issues in Fluorine-19 NMR, Steric effects and Protein folding.
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