PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7265525

[Normal range calculation: selection of the truncation coefficient for iterative truncation method with correction (author's tranl)].

T Usui
View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

EnzymesHumansMathematicsReference StandardsReference ValuesJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T Usui. 1981. [Normal range calculation: selection of the truncation coefficient for iterative truncation method with correction (author's tranl)].. https://pubmed.ncbi.nlm.nih.gov/7265525/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2026

How not to be seen: predicting unseen enzyme functions using contrastive learning.

MOTIVATION: Predicting enzyme function from its sequence is still an unsolved problem in the life sciences. Moreover, with the explosion of annotated genome data, we are inundated with potential enzymatic sequences that have not yet been biochemically characterized. While it is not possible to assign a not-yet-existing label to such a sequence, there is high value in placing the sequence as accurately as possible in known function space. Doing so can help provide more accurate falsifiable hypotheses for experimentalists wishing to characterize enzymes from specific functional families. RESULTS: Here we present a contrastive learning algorithm for predicting enzyme function from sequence. Our method, EnzPlacer, predicts the third, second, and first EC numbers for a protein whose fourth EC number is not in the training corpus. This novel prediction mechanism accurately places a protein sequence within a narrowed-down functional context, even if the precise function remains unknown. AVAILABILITY AND IMPLEMENTATION: EnzPlacer and data is available at https://github.com/drxiangma/EnzPlacer under a GPL3 license.

Enzymes↗
PubMed1999

Progress and variations in two-hybrid and three-hybrid technologies.

The original yeast two-hybrid system and its variants have proven to be effective tools for identification and analysis of protein-protein, protein-DNA and protein-RNA interactions. The two-hybrid assay is being applied to the entire complement of proteins of the yeast Saccharomyces cerevisiae to characterize the network of protein-protein interactions in the eukaryotic cell. The development of nontranscriptional cytosolic and membrane-associated two-hybrid methods has made it possible to detect and examine a number of protein-protein interactions in their normal cellular locations. Small-molecule hybrid systems have been developed which can be used to study protein-ligand interactions and to activate cellular processes by forcing protein associations.

Enzymes↗
PubMed1998

A novel method for determining kinetic parameters of dissociating enzyme systems.

The theoretical analysis has been presented for the kinetics of dissociating-associating enzyme-catalyzed reactions. On the basis of the kinetic equation of substrate reaction, a general procedure is developed for determining the kinetic constants of dissociating-associating enzyme reactions. By analyzing the experimental data of initial velocity and steady-state velocity as functions of enzyme and substrate concentration, all unknown kinetic parameters can be determined from several simple, sequential calculations. This method is simple and rigorous, and the required experiments may also not be difficult for most dissociating enzyme systems. Therefore, the present method should be a useful addition to the available methods for studying subunit dissociation of enzymes. In comparison to other physical methods, the advantage of this method is not only its usefulness in the study of self-associating reactions at very low protein concentration but its convenience in the study of substrate effects on subunit-subunit interactions.

Enzymes↗