Evidence map›Paper›PMID 20959105›Full record

ArticleBiophysical journal2010

NMR studies on domain diffusion and alignment in modular GB1 repeats.

Joseph D Walsh, Katlyn Meier, Rieko Ishima, Angela M Gronenborn

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

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26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Structural Basis of the Bivalency of the TRPV1 Agonist DkTx.Angewandte Chemie (International ed. in English) · 2024
    Article
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  6. Review
  7. Review
  8. The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90.Chembiochem : a European journal of chemical biology · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Decoding the components of dynamics in three-domain proteins.Journal of computational chemistry · 2014
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Joseph D WalshDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pennsylvania, USA.
Katlyn Meier
Rieko Ishima
Angela M Gronenborn

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modular proteins contain individual domains that are often connected by flexible, unstructured linkers. Using a model system based on the GB1 domain, we constructed tandem repeat proteins and investigated the rotational diffusion and long-range angular ordering behavior of individual domains by measuring NMR relaxation parameters and residual dipolar couplings. Although they display almost identical protein-solvent interfaces, each domain exhibits distinct rotational diffusion and alignment properties. The diffusion tensor anisotropy of the N-terminal domain (NTD) is D(‖)/D(⊥) = 1.5-1.6, similar to that of single-GB1 domains (D(‖)/D(⊥) = 1.6-1.7), whereas the value for the C-terminal domain (CTD) is D(‖)/D(⊥) = 2.0-2.2. In addition, the two domains have different rotational correlation times. These effects are observed for linkers of three to 24 residues, irrespective of linker length. The NTD and CTD also differ in their degree of magnetic alignment, even with a flexible linker of 18 residues, exhibiting D(a) values of 7.7 Hz and 9.7 Hz, respectively. Our results suggest that diffusion differences and long-range influences may persist in modular protein systems, even for systems that have highly flexible linkers and exhibit no domain-domain or domain-linker interactions.

Indexed as

Nuclear Magnetic Resonance, BiomolecularRepetitive Sequences, Amino AcidAmino Acid SequenceAnisotropyDiffusionModels, MolecularMolecular Sequence DataProteinsProtein Structure, TertiaryReproducibility of ResultsRotationProteins

Identifiers

PMID20959105
PMCPMC2955504

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.