APA

Westerhausen A., Kishi J. & Prockop D. J. (19900913). Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. : The Journal of biological chemistry.

Chicago

Westerhausen A, Kishi J and Prockop D J. 19900913. Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. : The Journal of biological chemistry.

Harvard

Westerhausen A., Kishi J. and Prockop D. J. (19900913). Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. : The Journal of biological chemistry.

MLA

Westerhausen A, Kishi J and Prockop D J. Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. : The Journal of biological chemistry. 19900913.