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Literature DB >> 1390678

1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.

Abstract

Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a single disulfide linkage. No evidence for any regular helical structure is found. Amide proton-solvent-exchange rate constants and 3JHN alpha coupling constants are evaluated.

Entities: Chemical Gene Species

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Year: 1992 PMID： 1390678 DOI： 10.1021/bi00152a030

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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Cited

20 in total

1. The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.

Authors: Giuliana Verdone; Alessandra Corazza; Paolo Viglino; Fabio Pettirossi; Sofia Giorgetti; Palma Mangione; Alessia Andreola; Monica Stoppini; Vittorio Bellotti; Gennaro Esposito
Journal: Protein Sci Date: 2002-03 Impact factor: 6.725

2. DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form.

Authors: Carlo Santambrogio; Stefano Ricagno; Matteo Colombo; Alberto Barbiroli; Francesco Bonomi; Vittorio Bellotti; Martino Bolognesi; Rita Grandori
Journal: Protein Sci Date: 2010-07 Impact factor: 6.725

3. The impact of window functions on NMR-based paramagnetic relaxation enhancement measurements in membrane proteins.

Authors: Wade D Van Horn; Andrew J Beel; Congbao Kang; Charles R Sanders
Journal: Biochim Biophys Acta Date: 2009-09-12

4. NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.

Authors: Monika Beerbaum; Martin Ballaschk; Natalja Erdmann; Christina Schnick; Anne Diehl; Barbara Uchanska-Ziegler; Andreas Ziegler; Peter Schmieder
Journal: J Biomol NMR Date: 2013-09-05 Impact factor: 2.835

5. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR.

Authors: Alessandra Corazza; Enrico Rennella; Paul Schanda; Maria Chiara Mimmi; Thomas Cutuil; Sara Raimondi; Sofia Giorgetti; Federico Fogolari; Paolo Viglino; Lucio Frydman; Maayan Gal; Vittorio Bellotti; Bernhard Brutscher; Gennaro Esposito
Journal: J Biol Chem Date: 2009-12-22 Impact factor: 5.157

1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.

1. The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.

2. DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form.

3. The impact of window functions on NMR-based paramagnetic relaxation enhancement measurements in membrane proteins.

4. NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.

5. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR.

6. Dynamics of free versus complexed β2-microglobulin and the evolution of interfaces in MHC class I molecules.

7. Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry.

8. Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.

9. Metal binding sheds light on mechanisms of amyloid assembly.

10. A regulatable switch mediates self-association in an immunoglobulin fold.