Bovine trypsin protein inhibitor is a relatively small globular peptide, therefore its structure is relatively simple, and it provides a good starting point to study the structure of globular proteins. The objectives of this exercise are to illustrate three of the more common secondary structures (a helix, b sheet, b turn) and to show how these structural components are a part of the folding which produces the tertiary structure. This exercise contains only one chapter.

Chapter 1 in PiPE format

After an over view of the tertiary structure, secondary structural components are identified and then some of the important forces that maintain the secondary and tertiary structures are shown.

Chapter 2 in MolSlide format

After an over view of the tertiary structure, secondary structural components are identified and then some of the important forces that maintain the secondary and tertiary structures are shown.

1.  References: A. Wlodawer, J. Walter, R. Huber, L. Sjolin, J. Mol. Biol., v. 180, 301, 1984; A. Wlodawer, J. Deisenhofer, R. Huber, J. Mol. Biol., v. 193, 145, 1987

This is a Presentation in Protein Explorer (PiPE) prepared with proteinexplorer.org. Development of Protein Explorer was supported by a grant to Eric Martz from the Division of Undergraduate Education of the US National Science Foundation.