Literature DB >> 101254

Allostery in an immunoglobulin light-chain dimer: a chemical relaxation study.

D Lancet, A Licht, I Pecht.   

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Year:  1978        PMID： 101254      PMCID： PMC1473885          DOI： 10.1016/S0006-3495(78)85365-X

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


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  4 in total

1.  The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme.

Authors:  K Kirschner; M Eigen; R Bittman; B Voigt
Journal:  Proc Natl Acad Sci U S A       Date:  1966-12       Impact factor: 11.205

2.  Hapten-induced allosteric transition in the light chain dimer of an immunoglobulin.

Authors:  D Lancet; A Licht; I Schechter; I Pecht
Journal:  Nature       Date:  1977-10-27       Impact factor: 49.962

3.  Thermodynamic and spectroscopic comparison of the binding sites of the mouse myeloma protein 315 and of its light chain dimer.

Authors:  A Licht; D Lancet; I Schechter; I Pecht
Journal:  FEBS Lett       Date:  1977-06-15       Impact factor: 4.124

4.  Binding of 2,4-dinitrophenyl derivatives by the light chain dimer obtained from immunoglobulin A produced by MOPC-315 mouse myeloma.

Authors:  I Schechter; E Ziv
Journal:  Biochemistry       Date:  1976-06-29       Impact factor: 3.162
  4 in total

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