Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c.
Clarkson
Michael W
MW
Department of Biochemistry and Biophysics, School of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599-7360, USA.
Lee
Andrew L
AL
D000409:Alanine / Q000235:genetics; D000818:Animals; D007865:Leeches; D008956:Models, Chemical; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D036103:Nanotechnology / Q000379:methods; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010649:Phenylalanine / Q000235:genetics; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics; D011506:Proteins; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000235:genetics; D015843:Serpins / Q000737:chemistry* / Q000235:genetics; D013816:Thermodynamics; D014364:Tryptophan / Q000235:genetics; D014633:Valine / Q000235:genetics
D021122:Protein Subunits; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins; C028656:eglin proteinase inhibitors; D010649:Phenylalanine; D014364:Tryptophan; D014633:Valine; D000409:Alanine