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Record W2887153055

Effect of solute-solvent interactions on protein stability and ligand binding

2017· dissertation· en· W2887153055 on OpenAlexafffund
Ikbae Son

Bibliographic record

VenueTSpace (University of Toronto) · 2017
Typedissertation
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Structure and Dynamics
Canadian institutionsUniversity of Toronto
FundersCanadian Institutes of Health Research
KeywordsLigand (biochemistry)ChemistryProtein stabilityStability (learning theory)SolventBiophysicsBiochemistryBiologyComputer scienceReceptor
DOInot available

Abstract

fetched live from OpenAlex

My doctoral thesis is aimed at characterizing the effect of solute–solvent interactions on protein stability and ligand binding events. To quantify non-specific protein–solvent interactions, we measured and analyzed partial molar volume and compressibility of proteins within a framework of statistical thermodynamic formalisms. We characterized the binding of tri-N-acetylglucosamine [(GlcNAc)3] and cAMP to lysozyme and cAMP-binding domain of EPAC1, respectively. Our volumetric measurements reveal that the protein–ligand complexes are less dynamic compared to their unbound states while complex formation is accompanied by the release of water of hydration to the bulk. To characterize protein–urea interactions, we determined and analyzed volumetric properties of four globular proteins at urea concentrations ranging from 0 to 8 M. We interpreted urea-dependent volumetric measurements in terms of the solvent exchange model in which the binding of urea to a protein proceeds with a release of two waters of hydration. Comparison of urea-dependent volumetric data for a folded protein with the similar data obtained on small molecules mimicking protein groups suggests the lack of cooperative effects involved in protein–urea interactions. Changes in volumetric properties associated with urea-induced unfolding transitions are consistent with solvent-accessible surface areas of unfolded proteins being roughly twice as large as those of their respective native states. Specifically, we reported the first experimental characterization of the thermodynamic profile of urea binding to a native protein. We measured the volumetric parameters of lysozyme as a function of urea within a temperature range of 18 to 45 ◦C. Based on the van’t Hoff analysis of the temperature dependence of the equilibrium constants for protein–urea binding events we evaluated the full thermodynamic profile of protein–urea interactions. Finally, we combined the experimental and theoretical approaches to investigate the influence of the urea on the binding of (GlcNAc)3 to lysozyme. Analysis of urea dependence of the binding free energy reveals that the protein–ligand binding reaction is governed by a close interplay between the free energy contributions of the excluded volume effect and direct solute–solvent interactions.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.001
metaresearch head score (Gemma)0.001
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.001
Threshold uncertainty score0.004

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0010.001
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0010.000
Open science0.0000.000
Research integrity0.0000.001
Insufficient payload (model declined to judge)0.0010.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.007
GPT teacher head0.260
Teacher spread0.253 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2017
Admission routes2
Has abstractyes

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