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Record W7067005832

Kinetics of the inhibition of calmodulin-dependent protein kinase II by pea protein-derived peptides

2004· dissertation· en· W7067005832 on OpenAlex

Why this work is in the frame

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

fundA Canadian funder is recorded on the work.
no affNo Canadian affiliation: this work is invisible to an affiliation-only frame.
No Canadian affiliation. An affiliation-only frame, the usual design, would never have seen this work. It is one of the works that make the case for inverting the frame.

Bibliographic record

VenueMspace (University of Manitoba) · 2004
Typedissertation
Languageen
FieldSocial Sciences
TopicColonial History and Postcolonial Studies
Canadian institutionsnot available
FundersNatural Sciences and Engineering Research Council of Canada
KeywordsPeptideCircular dichroismCalmodulinProtein kinase AKineticsEnzymeAmino acidPhosphorylationHydrolysis
DOInot available

Abstract

fetched live from OpenAlex

Calmodulin (CaM) is a ubiquitous protein present in all living cells and is involved in calcium-mediated activation of various physiologically important enzymes.Agents that bind to CaM can prevent activity of CaM-dependent protein kinase ll (CaMKll), an enzyme that has been implicaied in the initiation and propagation of chronic diseases.Agents that decrease or block the activity of CaMKll can reduce or eliminate excessive protein phosphorylation and, therefore, minimize or prevent associated pathological conditions.lnhibitors of CaM usually have either a net positive charge or a net hydrophobic character.Therefore, pea protein isolate with high levels of positively charged amino acids was enzymatically hydrolyzed to generate peptides with net positive charges.The peptides were separated on a cation-exchange column to obtain two peptide fractions that differed in level of positive charges.CaM-binding determination showed that fraction #2 had higher contents of basic amino acid residues and almost three times affinity for CaM when compared with fraction #1 .Enzyme inhibition kinetics was studied for peptides to see if they could inhibit CaMKll activity.lnhibition by the two peptide fractions followed a competitive manner and fraction #2 had a higher inhibition constant than fraction #1 .Fluorescence spectrophotometry and circular dichroism (CD) were used to determine the structural changes of CaM in the presence of enzyme and inhibitory peptides.The results showed thai interactions between CaM and inhibitory peptides led to the unfolding of CaM and exposure of previously buried hydrophobic groups.Peptide #2 was more effective than peptide #1 in causing unfolding of CaM.CD studies showed that the inhibitory peptides reduced the amount of c-helix siructure, a conformation that seems to be required for optimum interaction of CaM with target enzymes.Excessive unfolding of CaM by the inhibitory peptides led to increased interaction with CaMKll followed by unfolding of enzyme structure and reduction in enzyme activity.lt was concluded that pea protein-derived low molecular weight peptides with net positive charges interacted strongly and caused excessive unfolding of CaM, which reduced the ability of CaM to activate CaMKll; howeve this inhibition can be removed by increasing the concentrations of CaM. ACKNOWLEGMENTFirst and foremost, I would sincerely like to thank my

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.

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation 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 score0.765
Threshold uncertainty score0.957

Codex and Gemma teacher scores by category

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

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 head0.011
GPT teacher head0.217
Teacher spread0.206 · 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