title: Natively unfolded regions of the vertebrate fibrinogen molecule.
abstract: Although it has long been realized that a large portion of the fibrinogen alpha chain has little if any defined structure, the physiological significance of this flexible appendage remains mysterious.
authors.affiliation: Division of Biological Sciences, Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0634, USA. rdoolittle@ucsd.edu
authors.forename: Russell F
authors.initials: RF
authors.lastname: Doolittle
authors.forename: Justin M
authors.initials: JM
authors.lastname: Kollman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005176:Factor XIII / Q000378:metabolism; D005340:Fibrinogen / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding
chemical_list: D010446:Peptide Fragments; D005340:Fibrinogen; D005176:Factor XIII