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Literature DB >> 20465253

Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.

D Flemming Hansen¹, Philipp Neudecker, Lewis E Kay.

Abstract

A simple method is presented for quantifying Ile chi(2) rotamer distributions in proteins based on the measurement of Ile (13)C(delta1) chemical shifts. The methodology is well suited for applications involving very high molecular weight protein complexes, where other NMR parameters such as side-chain scalar coupling constants that report on dihedral angles cannot be measured or for studies of invisible, excited protein states, where chemical shifts are obtained from analysis of CPMG relaxation dispersion profiles. The utility of the approach is demonstrated by an application to the folding reaction of a mutant Fyn SH3 domain, where Ile side-chain structure and dynamics of an on-folding pathway intermediate state are studied.

Entities: Chemical Gene

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Year: 2010 PMID： 20465253 DOI： 10.1021/ja102090z

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

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Cited

45 in total

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Authors: Siavash Vahidi; Zev A Ripstein; Massimiliano Bonomi; Tairan Yuwen; Mark F Mabanglo; Jordan B Juravsky; Kamran Rizzolo; Algirdas Velyvis; Walid A Houry; Michele Vendruscolo; John L Rubinstein; Lewis E Kay
Journal: Proc Natl Acad Sci U S A Date: 2018-06-25 Impact factor: 11.205

10. Recognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein.

Authors: Alexander S Krois; Josephine C Ferreon; Maria A Martinez-Yamout; H Jane Dyson; Peter E Wright
Journal: Proc Natl Acad Sci U S A Date: 2016-03-14 Impact factor: 11.205

Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.

1. Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.

2. Suppression of conformational heterogeneity at a protein-protein interface.

3. Reversible inhibition of the ClpP protease via an N-terminal conformational switch.

4. Solid-state NMR study reveals collagen I structural modifications of amino acid side chains upon fibrillogenesis.

5. Interpreting protein structural dynamics from NMR chemical shifts.

Review 6. An introduction to NMR-based approaches for measuring protein dynamics.

Review 7. Protein design: Past, present, and future.

8. Pressure dependence of side chain ¹³C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH₂.

9. The physiological target for LeuRS translational quality control is norvaline.

10. Recognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein.