Leucine Side-Chain Conformation and Dynamics in Proteins from C-13 NMR Chemical Shifts

Frans A. A. Mulder*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

35 Citations (Scopus)

Abstract

The carbon nucleus of a substituent in the gauche position about a subtending dihedral angle experiences an NMR chemical shift of about 5 ppm relative to the same chemical group present in the trans position. We demonstrate that this “γ‐gauche effect” can be utilized to determine the conformation and extent of rotameric averaging for leucine amino acid side chains in the protein calbindin D9k. The success of this approach suggests that rules can be established to define the orientation of other side chains in proteins as well, offering an easy gauge of protein side‐chain flexibility, as well as avenues to advance protein structure determination by using side‐chain chemical shifts.
Original languageEnglish
Pages (from-to)1477-1479
Number of pages3
JournalChemBioChem
Volume10
Issue number9
DOIs
Publication statusPublished - 15-Jun-2009

Keywords

  • chemical shifts
  • NMR spectroscopy
  • protein dynamics
  • protein structures
  • structural biology
  • MAGNETIC-RESONANCE SPECTROSCOPY
  • DEUTERIUM SPIN PROBES
  • RELAXATION RATES
  • CALBINDIN D-9K
  • H-2
  • COUPLINGS
  • POLYMERS
  • MOTIONS
  • ALKANES

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