Magic-Angle Spinning Solid-State NMR Spectroscopy of the β1 Immunoglobulin Binding Domain of Protein G (GB1): 15N and 13C Chemical Shift Assignments and Conformational Analysis-Reference-Cited by-同舟云学术

Magic-Angle Spinning Solid-State NMR Spectroscopy of the β1 Immunoglobulin Binding Domain of Protein G (GB1): 15N and 13C Chemical Shift Assignments and Conformational Analysis

Published:2005-08-11 Issue:35 Volume:127 Page:12291-12305
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Franks W. Trent¹,Zhou Donghua H.¹,Wylie Benjamin J.¹,Money Brian G.¹,Graesser Daniel T.¹,Frericks Heather L.¹,Sahota Gurmukh¹,Rienstra Chad M.¹

Affiliation:

1. Contribution from the Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja044497e

Reference83 articles.

1. PROTOFIBRILS, PORES, FIBRILS, AND NEURODEGENERATION: Separating the Responsible Protein Aggregates from The Innocent Bystanders

2. High-resolution NMR of biological solids

3. Applications of solid state NMR to the structural characterization of amyloid fibrils: methods and results

4. Crystal Versus Solution Structures of Enzymes: NMR Spectroscopy of a Crystalline Serine Protease

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