MétaCan
Menu
Back to cohort
Record W2050454782 · doi:10.2174/092986611794653950

Can Enzyme Engineering Benefit from the Modulation of Protein Motions? Lessons Learned from NMR Relaxation Dispersion Experiments

2011· review· en· W2050454782 on OpenAlexaff
Nicolas Doucet

Bibliographic record

VenueProtein and Peptide Letters · 2011
Typereview
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Structure and Dynamics
Canadian institutionsInstitut National de la Recherche Scientifique
Fundersnot available
KeywordsProtein engineeringRational designSaturated mutagenesisDirected evolutionMutagenesisProtein designDihydrofolate reductaseProtein dynamicsFunction (biology)Nuclear magnetic resonance spectroscopyChemistryProtein structureEnzymeComputational biologyNanotechnologyBiochemistryMaterials scienceBiologyStereochemistry

Abstract

fetched live from OpenAlex

Despite impressive progress in protein engineering and design, our ability to create new and efficient enzyme activities remains a laborious and time-consuming endeavor. In the past few years, intricate combinations of rational mutagenesis, directed evolution and computational methods have paved the way to exciting engineering examples and are now offering a new perspective on the structural requirements of enzyme activity. However, these structure-function analyses are usually guided by the time-averaged static models offered by enzyme crystal structures, which often fail to describe the functionally relevant ‘invisible states’ adopted by proteins in space and time. To alleviate such limitations, NMR relaxation dispersion experiments coupled to mutagenesis studies have recently been applied to the study of enzyme catalysis, effectively complementing ‘structure-function’ analyses with ‘flexibility-function’ investigation. In addition to offering quantitative, site-specific information to help characterize residue motion, these NMR methods are now being applied to enzyme engineering purposes, providing a powerful tool to help characterize the effects of controlling long-range networks of flexible residues affecting enzyme function. Recent advancements in this emerging field are presented here, with particular attention to mutagenesis reports highlighting the relevance of NMR relaxation dispersion tools in enzyme engineering. Keywords: CPMG, enzyme catalysis, NMR spectroscopy, protein engineering, relaxation dispersion, residue motion, Protein Motions, NMR Relaxation, rational mutagenesis, structure-function, flexibility-function, dispersion tools, biocatalysts, semi-random mutagenesis, de novo, nanoscale machines, dihydrofolate reductase, adenylate kinase, amino acid networks, enablers, disruptors, dispersion experiments, Cyclophilin A, Pin1, Ribonuclease A, drug development and nanotechnologyCPMG, enzyme catalysis, NMR spectroscopy, protein engineering, relaxation dispersion, residue motion, Protein Motions, NMR Relaxation, rational mutagenesis, structure-function, flexibility-function, dispersion tools, biocatalysts, semi-random mutagenesis, de novo, nanoscale machines, dihydrofolate reductase, adenylate kinase, amino acid networks, enablers, disruptors, dispersion experiments, Cyclophilin A, Pin1, Ribonuclease A, drug development and nanotechnology

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)0.002
metaresearch head score (Gemma)0.005
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Not applicable · Consensus signal: none
GenreCandidate signal: Review · Consensus signal: Review
Teacher disagreement score0.002
Threshold uncertainty score0.013

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0020.005
Meta-epidemiology (narrow)0.0010.000
Meta-epidemiology (broad)0.0010.001
Bibliometrics0.0000.000
Science and technology studies0.0000.003
Scholarly communication0.0010.006
Open science0.0010.001
Research integrity0.0020.004
Insufficient payload (model declined to judge)0.0010.001

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 head0.034
GPT teacher head0.268
Teacher spread0.233 · 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 designNot applicable
Domainnot available
GenreReview

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

Citations17
Published2011
Admission routes1
Has abstractyes

Explore more

Same venueProtein and Peptide LettersSame topicProtein Structure and DynamicsFrench-language works237,207