Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy-Reference-Cited by-同舟云学术

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Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy

Published:1992-07-16 Issue:23 Volume:31 Page:5237-5245
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Stockman Brian J.,Scahill Terrence A.,Roy Melinda,Ulrich Eldon L.,Strakalaitis Nancy A.,Brunner David P.,Yem Anthony W.,Deibel Martin R.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00138a001

Reference40 articles.

1. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

2. Interleukin 1 receptor antagonist. A new member of the interleukin 1 family.

3. An efficient 3D NMR technique for correlating the proton and15N backbone amide resonances with the α-carbon of the preceding residue in uniformly15N/13C enriched proteins

4. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

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2. Effect Of Benzyl Alcohol on Recombinant Human Interleukin-1 Receptor Antagonist Structure and Hydrogen–Deuterium Exchange;Journal of Pharmaceutical Sciences;2011-10

3. Denaturant-Dependent Conformational Changes in a β-Trefoil Protein: Global and Residue-Specific Aspects of an Equilibrium Denaturation Process;Biochemistry;2009-10-29

4. Refined Crystal Structure of the Interleukin-1 Receptor Antagonist;European Journal of Biochemistry;2008-06-28

5. Conformation and Side Chains Environments of Recombinant Human Interleukin-1 Receptor Antagonist (rh-IL-1ra) Probed by Raman, Raman Optical Activity, and UV-Resonance Raman Spectroscopy;Journal of Pharmaceutical Sciences;2008-06

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