Contributions from all over widely distributed residues in thymosin beta-4 affect the kinetics and stability of actin binding

Annals of the New York Academy of Sciences

Volumn 1112, Issue , 2007, Pages 38-44

  Au, Joshua K ^a   De La Cruz, Enrique M ^a   Safer, Daniel ^b  

^a YALE UNIVERSITY   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Actin; Affinity; Fluorescence; Kinetics; Mutagenesis; Rapid mixing; Stopped flow; Thymosin 4

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE MAGNESIUM; ETHYLENEDIAMINE DERIVATIVE; ISOLEUCINE; LEUCINE; LYSINE; MUTANT PROTEIN; N IODOACETYL N 9 (5 SULFO 1 NAPHTHYL)ETHYLENEDIAMINE; PROLINE; PROTEIN SUBUNIT; THYMOSIN BETA4; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL TISSUE; BINDING AFFINITY; BINDING KINETICS; CIS TRANS ISOMERISM; COMPLEX FORMATION; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTRICITY; EQUILIBRIUM CONSTANT; FLUORESCENCE; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR STABILITY; MUTATION; NONHUMAN; PROTEIN BINDING; PROTEIN LOCALIZATION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS; WILD TYPE;

EID: 35348953071     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1196/annals.1415.015     Document Type: Conference Paper

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