Combined Use of NMR Relaxation Measurements and Hydrodynamic Calculations To Study Protein Association. Evidence for Tetramers of Low Molecular Weight Protein Tyrosine Phosphatase in Solution-Reference-Cited by-同舟云学术

Combined Use of NMR Relaxation Measurements and Hydrodynamic Calculations To Study Protein Association. Evidence for Tetramers of Low Molecular Weight Protein Tyrosine Phosphatase in Solution

Published:2002-12-28 Issue:4 Volume:125 Page:916-923
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bernadó Pau¹,Åkerud Tomas¹,García de la Torre José¹,Akke Mikael¹,Pons Miquel¹

Affiliation:

1. Contribution from the Departament de Química Orgànica, Universitat de Barcelona, Martí i Franquès, 1-11, 08028, Barcelona, Spain, Laboratori de RMN de Biomolècules, Parc Científic de Barcelona, Josep Samitier, 1-5, 08028,Barcelona, Spain, Department of Biophysical Chemistry, Lund University, Box 124, SE-22100 Lund, Sweden, Structural Chemistry, Biovitrum, Stockholm, Sweden, and Departamento de Química Física, Facultad de Química, Universidad de Murcia, 30071, Múrcia, Spain

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja027836h

Reference42 articles.

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3. The role of tetramerization in p53 function

4. Switching Signals On or Off by Receptor Dimerization

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