Westerhausen, A <br/><br/>
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.  [electronic resource] 

 -  The Journal of biological chemistry  Aug 1990 
 - 13995-4000 p.  digital 
<br/><br/> Publication Type: Case Reports; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Base Sequence<br/>Cells, Cultured<br/>Codon--genetics<br/>DNA--genetics<br/>Fibroblasts--metabolism<br/>Glycine<br/>Humans<br/>Infant, Newborn<br/>Infant, Premature<br/>Male<br/>Models, Structural<br/>Molecular Sequence Data<br/>Mutation<br/>Oligonucleotide Probes<br/>Osteogenesis Imperfecta--genetics<br/>Polymerase Chain Reaction<br/>Procollagen--genetics<br/>Protein Conformation<br/>Protein Denaturation<br/>Serine<br/>Skin--metabolism<br/>Templates, Genetic