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Title of Journal: Biomol NMR Assign

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Abbravation: Biomolecular NMR Assignments

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Springer Netherlands

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DOI

10.1007/1-84628-133-4_3

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ISSN

1874-270X

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Superscript1/SuperscriptH Superscript13/Su

Authors: Thomas Schallus Christian Edlich Gunter Stier Claudia MuhleGoll
Publish Date: 2007/05/10
Volume: 1, Issue: 1, Pages: 41-43
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Abstract

The family of CRP proteins comprises three members which are composed of two LIM domains separated by a long linker of more than 50 residues We determined the structure of the muscle variant MLP CRP3 by nuclear magnetic resonance and show that the two LIM domains are independent of each other

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Other Papers In This Journal:
  1. Letter to the Editor: Resonance assignment of SlyD from E. coli
  2. NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1
  3. A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216)
  4. 1 H, 13 C, 15 N resonance assignment of the chitin-binding protein CBP21 from Serratia marcescens
  5. Backbone nuclear magnetic resonance assignment of human deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase)
  6. Backbone and sidechain 1 H, 13 C and 15 N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid
  7. 1 H, 13 C and 15 N assignment of the C-terminal domain of GNA2132 from Neisseria meningitidis
  8. 1 H, 13 C, 15 N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the Hv GR-RBP1 protein involved in the regulation of barley ( Hordeum vulgare L.) senescence
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