title: FHA domain-ligand interactions: importance of integrating chemical and biological approaches.
abstract: Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions.
authors.affiliation: Biophysics Program, The Ohio State University, Columbus, Ohio 43210, USA.
authors.forename: Anjali
authors.initials: A
authors.lastname: Mahajan
authors.forename: Chunhua
authors.initials: C
authors.lastname: Yuan
authors.forename: Brietta L
authors.initials: BL
authors.lastname: Pike
authors.forename: Jörg
authors.initials: J
authors.lastname: Heierhorst
authors.forename: Chi-Fon
authors.initials: CF
authors.lastname: Chang
authors.forename: Ming-Daw
authors.initials: MD
authors.lastname: Tsai
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism; D051858:Forkhead Transcription Factors / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D010769:Phosphothreonine / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D018797:Cell Cycle Proteins; C464906:Fkh1 protein, S cerevisiae; D051858:Forkhead Transcription Factors; D008024:Ligands; D029701:Saccharomyces cerevisiae Proteins; D010769:Phosphothreonine