A specific chymotryptic inhibitor was used to validate the enzyme's role.
A synthetic peptide substrate was used to measure chymotryptic activity quantitatively.
After chymotryptic digestion, the resulting peptides were analyzed by mass spectrometry.
Analysis of the chymotryptic digest revealed a novel post-translational modification.
Chymotryptic cleavage is often used in proteomic studies to identify proteins.
Chymotryptic digestion can be used to generate peptides for antibody production.
Chymotryptic digestion is a common method for protein sequencing.
Comparing the chymotryptic digests provided insights into the protein's structure.
He hypothesized that the chymotryptic fragments would reveal key binding domains.
Specific inhibitors can effectively block the chymotryptic activity of the enzyme.
The analysis focused on identifying the chymotryptic cleavage sites within the protein sequence.
The chymotryptic activity of the protease was measured in a cell-based assay.
The chymotryptic activity was significantly reduced in the mutant enzyme.
The chymotryptic cleavage site was located near the C-terminus of the protein.
The chymotryptic cleavage sites were predicted using bioinformatics tools.
The chymotryptic digestion was followed by HPLC separation of the resulting peptides.
The chymotryptic digestion was performed under denaturing conditions.
The chymotryptic enzyme displays a preference for aromatic amino acids.
The chymotryptic fragments were analyzed using electrospray ionization mass spectrometry.
The chymotryptic fragments were analyzed using ion trap mass spectrometry.
The chymotryptic fragments were analyzed using matrix-assisted laser desorption/ionization mass spectrometry.
The chymotryptic fragments were analyzed using tandem mass spectrometry.
The chymotryptic fragments were analyzed using time-of-flight mass spectrometry.
The chymotryptic fragments were identified by their unique masses and retention times.
The chymotryptic fragments were purified by high-performance liquid chromatography.
The chymotryptic fragments were subjected to amino acid composition analysis.
The chymotryptic fragments were used to generate a peptide fingerprint.
The chymotryptic fragments were used to generate a protein degradation pathway.
The chymotryptic fragments were used to generate a protein interaction map.
The chymotryptic fragments were used to generate a protein regulatory network.
The chymotryptic fragments were used to generate a protein structure model.
The chymotryptic map showed that the protein was heavily glycosylated.
The chymotryptic peptides were analyzed using Edman degradation.
The chymotryptic peptides were identified by database searching using Mascot.
The chymotryptic peptides were separated using reverse-phase chromatography.
The chymotryptic peptides were sequenced using a de novo sequencing approach.
The chymotryptic peptides were then subjected to further analysis by LC-MS/MS.
The chymotryptic peptides were used to generate a protein database search.
The chymotryptic specificity was altered by site-directed mutagenesis.
The data indicated that the protein undergoes chymotryptic processing in vivo.
The data revealed a complex network of chymotryptic interactions within the cell.
The data suggested that chymotryptic processing is essential for protein maturation.
The enzyme showed a preference for chymotryptic cleavage after tyrosine residues.
The enzyme showed increased chymotryptic activity at elevated temperatures.
The enzyme's chymotryptic activity was affected by the presence of detergents.
The enzyme's chymotryptic activity was affected by the presence of salts.
The enzyme's chymotryptic activity was dependent on the presence of cofactors.
The enzyme's chymotryptic activity was dependent on the presence of metal ions.
The enzyme's chymotryptic activity was essential for its biological function.
The enzyme's chymotryptic activity was essential for its proteolytic function.
The enzyme's chymotryptic activity was inhibited by specific antibodies.
The enzyme's chymotryptic activity was inhibited by specific peptides.
The enzyme's chymotryptic activity was inhibited by the presence of heavy metals.
The enzyme's chymotryptic activity was measured using a fluorogenic substrate.
The enzyme's chymotryptic activity was regulated by post-translational modifications.
The enzyme's substrate specificity was determined using a chymotryptic library.
The experiment evaluated the effects of various additives on chymotryptic efficiency.
The experiment involved labeling the protein prior to chymotryptic fragmentation.
The method allows for the rapid identification of chymotryptic cleavage products.
The modified protein exhibited altered chymotryptic cleavage patterns.
The mutation altered the protein's susceptibility to chymotryptic cleavage.
The protein was cleaved by chymotrypsin, yielding several chymotryptic fragments.
The protein's conformation influenced its susceptibility to chymotryptic cleavage.
The protein's degradation was initiated by a chymotryptic cleavage event.
The purified protein was subjected to chymotryptic hydrolysis for peptide analysis.
The recombinant protein was subjected to chymotryptic fingerprinting.
The researchers developed a new assay to measure chymotryptic activity in vitro.
The researchers investigated the effect of pH on chymotryptic digestion.
The researchers used a chymotryptic approach to study protein folding dynamics.
The researchers used a chymotryptic digest to confirm the protein's identity.
The researchers used a chymotryptic digest to map the acetylation sites in the protein.
The researchers used a chymotryptic digest to map the disulfide bonds in the protein.
The researchers used a chymotryptic digest to map the glycosylation sites in the protein.
The researchers used a chymotryptic digest to map the phosphorylation sites in the protein.
The researchers used a chymotryptic digest to map the sumoylation sites in the protein.
The researchers used a chymotryptic digest to map the ubiquitination sites in the protein.
The results highlighted the versatility of chymotryptic digestion in proteomics research.
The sequence coverage was improved by combining tryptic and chymotryptic digests.
The study aimed to identify novel chymotryptic substrates in the cellular extract.
The study aimed to identify novel substrates for chymotryptic enzymes.
The study aimed to identify the physiological substrates of this chymotryptic enzyme.
The study compared the chymotryptic digestion patterns of different protein isoforms.
The study demonstrated the importance of chymotryptic activity in bacterial pathogenesis.
The study focused on identifying the endogenous inhibitors of chymotryptic enzymes.
The study found that chymotryptic activity was decreased in aging cells.
The study found that chymotryptic activity was decreased in neurodegenerative diseases.
The study found that chymotryptic activity was increased in autoimmune diseases.
The study found that chymotryptic activity was increased in inflammatory conditions.
The study found that chymotryptic activity was increased in response to stress.
The study investigated the role of chymotryptic activity in cancer cell invasion.
The study investigated the role of chymotryptic activity in protein aggregation.
The study investigated the role of chymotryptic activity in protein degradation.
The study investigated the role of chymotryptic activity in protein folding.
The study investigated the role of chymotryptic activity in protein trafficking.
The study investigated the role of chymotryptic activity in protein turnover.
The study uncovered a novel regulatory mechanism of chymotryptic activity.
Understanding the chymotryptic degradation pathway is key to drug design.
We investigated the role of chymotryptic activity in extracellular matrix remodeling.
We optimized the chymotryptic digestion conditions for optimal peptide recovery.
We used a chymotryptic peptide mapping approach to characterize the protein variant.