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Record W2071866837 · doi:10.1366/0003702001950652

Examination of the Effect of Heating on the Secondary Structure of Avidin and Avidin—Biotin Complex by Resolution-Enhanced Two-Dimensional Infrared Correlation Spectroscopy

2000· article· en· W2071866837 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.

affAt least one author lists a Canadian institution in the pinned OpenAlex snapshot.

Bibliographic record

VenueApplied Spectroscopy · 2000
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicBiotin and Related Studies
Canadian institutionsMcGill University
Fundersnot available
KeywordsAvidinChemistryBiotinAnalytical Chemistry (journal)Infrared spectroscopyAntiparallel (mathematics)Fourier transform infrared spectroscopySpectroscopyProtein secondary structureCrystallographyChromatographyOpticsOrganic chemistryBiochemistry

Abstract

fetched live from OpenAlex

The Fourier transform infrared (FT-IR) spectra of avidin dissolved in D 2 O in the absence and the presence of biotin were recorded as a function of temperature over the range of 25–95 °C. At ambient temperature, the spectra revealed differences in secondary structure between uncomplexed avidin and avidin complexed to biotin. In the presence of biotin, avidin underwent slower H–D exchange, demonstrating that when complexed to biotin, avidin adopts a more compact structure that is less accessible to solvent molecules. In addition, examination of the amide I' band in the spectrum of the avidin–biotin complex revealed the presence of a new intramolecular β-sheet structure that is less exposed to solvent. Upon heating to 85 °C, aggregation of avidin occurred with the formation of extended intermolecular antiparallel β-sheet structures. When avidin was complexed to biotin, significant changes in its secondary structure were observed with increasing temperature, but the majority of these changes were found to be reversible upon decreasing the temperature, and no spectral bands associated with aggregate formation were observed over the temperature range examined. The effect of increasing temperature on the secondary structure of avidin in the presence and absence of biotin was further investigated by two-dimensional infrared (2D-IR) correlation spectroscopy. The 2D analysis of the spectra of the avidin–biotin complex was facilitated by the use of Fourier self-deconvolved spectra to generate the synchronous and asynchronous 2D contour maps, providing very sharp and well-resolved cross peaks. Examination of the synchronous and asynchronous contour maps generated from the IR spectra of avidin recorded as a function of increasing temperature revealed that the unfolding of α-helical structures and the disruption of turns preceded the unfolding of the β-sheet structures within the avidin. Subsequently, the unfolded protein formed intermolecular antiparallel β-sheet structures. The resultant β-sheet structures did not change upon cooling of the solution to ambient temperature. The avidin–biotin complex unfolded via a different pathway, following a sequence of events where the extended β-sheet structure unfolds first, followed by the unfolding of α-helical structures. This behavior in turn is followed by an increase in the antiparallel β-sheet structures. Upon cooling of the solution, the avidin–biotin complex refolded via the same pathway. These studies reveal the potential benefit of employing resolution-enhanced two-dimensional (RE-2D) IR correlation spectroscopy in the study of protein dynamics.

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 score0.014
Threshold uncertainty score0.453

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 studies0.0000.000
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 head0.003
GPT teacher head0.218
Teacher spread0.215 · 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