The Serine Protease Collection (SP) explores the structure and function of protease enzymes, which catalyze the cleavage of peptide bonds, the bonds that join amino acids together to form proteins. The active site of serine proteases contains three critical amino acids: serine, histidine and aspartate. These residues are often referred to as the "catalytic triad."
Models in this Collection
- α-carbon Backbone Chymotrypsin
- α-carbon Backbone Elastase
- α-carbon Backbone Trypsin
- Spacefill Chymotrypsin
- Spacefill Backbone Elastase
- Spacefill Backbone Trypsin
Requesting this Model
Loan Time Frame: 3 weeks
- Use the calendar below to select a three week loan. Available times are shown in green. Select a date one week prior to the date you want the model to arrive. After selecting your time period, select checkout and complete the booking details.
- This loan includes both delivery and return shipping time. Please make sure to plan time (approximately one week) for us to deliver the model to you. You can expect the model to arrive approximately one week following the first day of the requested loan period.
- Use the calendar below to select a three week loan. Available times are shown in green. Select the date you want to pick up the model. After selecting your time period, select checkout and complete the booking details.
Requesting Other Models
You may schedule one copy of a model for three weeks. Due to limited resources, we are unable to send multiple copies or additional materials.
If you would like to request a loan of a different model for the same time frame you may add this to your cart. Up to three different types of models may be checked out at one time. You will need to fill out a separate request for model loans with a different time frame.
Please contact us at firstname.lastname@example.org with any questions about the lending process or the availability of models.
Contact Margaret Franzen at email@example.com or (414) 277-2824 with questions about the models, teaching resources or educational content.