![Relating particle formation to salt‐ and pH‐dependent phase separation of non‐native aggregates of alpha‐chymotrypsinogen a - Journal of Pharmaceutical Sciences Relating particle formation to salt‐ and pH‐dependent phase separation of non‐native aggregates of alpha‐chymotrypsinogen a - Journal of Pharmaceutical Sciences](https://jpharmsci.org/cms/attachment/fc2bf790-0d06-4f76-8ae0-a0ae98648ff3/gr1.jpg)
Relating particle formation to salt‐ and pH‐dependent phase separation of non‐native aggregates of alpha‐chymotrypsinogen a - Journal of Pharmaceutical Sciences
![Studies of the chymotrypsinogen family. IV. The conversion of chymotrypsinogen A to alpha-chymotrypsin. | PNAS Studies of the chymotrypsinogen family. IV. The conversion of chymotrypsinogen A to alpha-chymotrypsin. | PNAS](https://www.pnas.org/cms/10.1073/pnas.54.5.1412/asset/bb1ed06e-e27a-4d65-a22e-c8f28947cbd4/assets/pnas.54.5.1412.fp.png)
Studies of the chymotrypsinogen family. IV. The conversion of chymotrypsinogen A to alpha-chymotrypsin. | PNAS
![SOLVED: The isoelectric point, pI, of the protein chymotrypsinogen A is 9.1 while that of peroxidase is 7.2 What is the net charge of chymotrypsinogen at pH 5.1 What is the net SOLVED: The isoelectric point, pI, of the protein chymotrypsinogen A is 9.1 while that of peroxidase is 7.2 What is the net charge of chymotrypsinogen at pH 5.1 What is the net](https://cdn.numerade.com/ask_images/03999c872fb04acba7b5b791a1bd8f42.jpg)
SOLVED: The isoelectric point, pI, of the protein chymotrypsinogen A is 9.1 while that of peroxidase is 7.2 What is the net charge of chymotrypsinogen at pH 5.1 What is the net
![Engineered ChymotrypsiN for Mass Spectrometry-Based Detection of Protein Glycosylation | ACS Chemical Biology Engineered ChymotrypsiN for Mass Spectrometry-Based Detection of Protein Glycosylation | ACS Chemical Biology](https://pubs.acs.org/cms/10.1021/acschembio.9b00506/asset/images/large/cb9b00506_0007.jpeg)
Engineered ChymotrypsiN for Mass Spectrometry-Based Detection of Protein Glycosylation | ACS Chemical Biology
![Aggregation of α-Chymotrypsinogen A in Aqueous Solutions Aaron Aziz Advisor: Dr. Yun Liu Colleague: Dr. Jiang Du. - ppt download Aggregation of α-Chymotrypsinogen A in Aqueous Solutions Aaron Aziz Advisor: Dr. Yun Liu Colleague: Dr. Jiang Du. - ppt download](https://slideplayer.com/7441211/24/images/slide_1.jpg)
Aggregation of α-Chymotrypsinogen A in Aqueous Solutions Aaron Aziz Advisor: Dr. Yun Liu Colleague: Dr. Jiang Du. - ppt download
![Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins | Scientific Reports Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41598-020-65696-5/MediaObjects/41598_2020_65696_Fig1_HTML.png)
Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins | Scientific Reports
![RCSB PDB - 2CGA: BOVINE CHYMOTRYPSINOGEN A. X-RAY CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF A NEW CRYSTAL FORM AT 1.8 ANGSTROMS RESOLUTION RCSB PDB - 2CGA: BOVINE CHYMOTRYPSINOGEN A. X-RAY CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF A NEW CRYSTAL FORM AT 1.8 ANGSTROMS RESOLUTION](https://files.rcsb.org/pub/pdb/validation_reports/cg/2cga/2cga_multipercentile_validation.png)
RCSB PDB - 2CGA: BOVINE CHYMOTRYPSINOGEN A. X-RAY CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF A NEW CRYSTAL FORM AT 1.8 ANGSTROMS RESOLUTION
1CHG: Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation
![Macromolecular crowding stabilises native structure of α-chymotrypsinogen-A against hexafluoropropanol-induced aggregates - ScienceDirect Macromolecular crowding stabilises native structure of α-chymotrypsinogen-A against hexafluoropropanol-induced aggregates - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0141813020342409-ga1.jpg)
Macromolecular crowding stabilises native structure of α-chymotrypsinogen-A against hexafluoropropanol-induced aggregates - ScienceDirect
![SOLVED: The linear retention data for the protein G-chymotrypsinogen A (pl-9.0) at pH 6.0 on a strong cation exchanger (S mm diameter by 5 cm in length) is plotted on the accompanying SOLVED: The linear retention data for the protein G-chymotrypsinogen A (pl-9.0) at pH 6.0 on a strong cation exchanger (S mm diameter by 5 cm in length) is plotted on the accompanying](https://cdn.numerade.com/ask_images/934e07276ddb457593260ab35d9905a4.jpg)