Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings

G. Bouvignies, P. Bernado, Sebastian Meier, K. Cho, S. Grzesiek, R. Bruschweiler, M. Blackledge

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Despite their importance for biological activity, slower molecular motions beyond the nanosecond range remain poorly understood. We have assembled an unprecedented set of experimental NMR data, comprising up to 27 residual dipolar couplings per amino acid, to define the nature and amplitude of backbone motion in protein G using the Gaussian axial fluctuation model in three dimensions. Slower motions occur in the loops, and in the beta-sheet, and are absent in other regions of the molecule, including the a-helix. In the beta-sheet an alternating pattern of dynamics along the pepticle sequence is found to form a long-range network of slow motion in the form of a standing wave extending across the beta-sheet, resulting in maximal conformational sampling at the interaction site. The alternating nodes along the sequence match the alternation of strongly hydrophobic side chains buried in the protein core. Confirmation of the motion is provided through extensive cross-validation and by independent hydrogen-bond scalar coupling analysis that shows this motion to be correlated. These observations strongly suggest that dynamical information can be transmitted across hydrogen bonds and have important implications for understanding collective motions and long-range information transfer in proteins.
Original languageEnglish
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number39
Pages (from-to)13885-13890
Number of pages6
ISSN0027-8424
DOIs
Publication statusPublished - 2005
Externally publishedYes

Keywords

  • Amino Acids
  • Bacterial Proteins
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Motion
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary
  • Proteins
  • IgG Fc-binding protein, Streptococcus
  • amino acid
  • alpha helix
  • article
  • beta sheet
  • dipole
  • hydrogen bond
  • hydrophobicity
  • molecular dynamics
  • motion
  • nuclear magnetic resonance
  • priority journal
  • protein analysis
  • protein conformation
  • protein interaction
  • statistical model
  • Hydrophobicity
  • Correlated
  • Protein dynamics
  • Slow motions
  • PROTEINS
  • MULTIDISCIPLINARY
  • BACKBONE DYNAMICS
  • NMR RELAXATION
  • STRUCTURAL GENOMICS
  • ORDER PARAMETERS
  • HIGH-ACCURACY
  • BIOMOLECULES
  • CATALYSIS
  • MODEL
  • MACROMOLECULES
  • SPECTROSCOPY
  • protein dynamics
  • slow motions
  • correlated
  • dipolar scalar coupling
  • hydrogen-bond scalar coupling
  • alpha-helix
  • beta-sheet
  • proteins
  • 10060, Biochemistry studies - General
  • 10064, Biochemistry studies - Proteins, peptides and amino acids
  • NMR imaging clinical techniques, spectrum analysis techniques, diagnostic techniques
  • Biochemistry and Molecular Biophysics

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