High-throughput ligand discovery reveals a sitewise gradient of diversity in broadly evolved hydrophilic fibronectin domains

PLoS ONE

Volumn 10, Issue 9, 2015, Pages

  Woldring, Daniel R ^a   Holec, Patrick V ^a   Zhou, Hong ^a   Hackel, Benjamin J ^a  

^a University of Minnesota   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; PROTEOME; COMPLEMENTARITY DETERMINING REGION; LIGAND; PEPTIDE LIBRARY;

AMINO ACID DIVERSITY SITEWISE GRADIENT; AMINO ACID SUBSTITUTION; ANALYTICAL PARAMETERS; ARTICLE; BINDING AFFINITY; BINDING SITE; CHEMICAL PARAMETERS; COMBINATORIAL LIBRARY; COMPLEMENTARITY BIAS; CONTROLLED STUDY; ENTROPY; HIGH THROUGHPUT SEQUENCING; HYDROPHILICITY; INTERMOLECULAR INTERACTION; INTRAMOLECULAR INTERACTION; LOOP LLENGTH VARIATION; MOLECULAR EVOLUTION; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; PROBABILITY; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN STABILITY; SEQUENCE ANALYSIS; SHANNON ENTROPY; WILD TYPE CONSTRAINT; COMPLEMENTARITY DETERMINING REGION; METABOLISM; MOLECULAR MODEL; PEPTIDE LIBRARY; PROTEIN TERTIARY STRUCTURE;

COMPLEMENTARITY DETERMINING REGIONS; FIBRONECTINS; LIGANDS; MODELS, MOLECULAR; PEPTIDE LIBRARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS, PROTEIN;

EID: 84946594789     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0138956     Document Type: Article

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