Mapping Oxygen Accessibility to Ribonuclease A Using High-Resolution NMR Relaxation Spectroscopy

Ching Ling Teng, Robert G. Bryant

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Paramagnetic contributions to nuclear magnetic spin-lattice relaxation rate constant induced by freely diffusing molecular oxygen measured at hundreds of different protein proton sites provide a direct means for characterizing the exploration of the protein by oxygen. This report focuses on regions of ribonuclease A where the rate constant enhancements are either quite large or quite small. We find that there are several regions of enhanced oxygen affinity for the protein both on the surface and in interior pockets where sufficient free volume permits. Oxygen has weak associative interactions with a number of surface crevices that are generally between secondary structural elements of the protein fold. Several regions near the surface have higher than expected accessibility to oxygen indicating that structural fluctuations in the protein provide intermolecular access. Oxygen penetrates part of the hydrophobic interior, but affinity does not correlate simply with hydrophobicity indices. Oxygen is excluded from regions of high interior packing density and a few surface sites where x-ray diffraction data have indicated the presence of specific hydration with high occupancy.

Original languageEnglish (US)
Pages (from-to)1713-1725
Number of pages13
JournalBiophysical Journal
Volume86
Issue number3
DOIs
StatePublished - Mar 2004
Externally publishedYes

Fingerprint

Pancreatic Ribonuclease
Magnetic Resonance Spectroscopy
Oxygen
Proteins
Hydrophobic and Hydrophilic Interactions
Protons
X-Rays

ASJC Scopus subject areas

  • Biophysics

Cite this

Mapping Oxygen Accessibility to Ribonuclease A Using High-Resolution NMR Relaxation Spectroscopy. / Teng, Ching Ling; Bryant, Robert G.

In: Biophysical Journal, Vol. 86, No. 3, 03.2004, p. 1713-1725.

Research output: Contribution to journalArticle

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