Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Application of nuclear magnetic-resonance spectroscopy to proteins

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Griffin, John
  • Furie, B.
  • Schechter, A. N.

publication date

  • 1975

journal

  • Biochimie  Journal

abstract

  • The active sites of enzymes can be studied in great detail using nuclear magnetic resonance spectroscopy. The determination of pKa values of active site histidine residues in bovine pancreatic ribonuclease and the characterization of the binding of peptide hormones to carrier proteins are two such examples. The study of the active site of staphylococcal nuclease is another example and is presented in detail in this paper. The structure of 3'5'-thymidine diphosphate bound in the active site of staphylococcal nuclease has been studied by measuring the relaxation rate enhancement of substrate analog nuclei by a paramagnetic metal ion. The lanthanide ion, Gd(III), was substituted for Ca(II) in the formation of the ternary complex of nuclease: Gd(III) : 3'5'-thymidine diphosphate. Measurements were made of the transverse relaxation rates of protons and the longitudinal and transverse relaxation rates of the phosphorus nuclei of bound nucleotide. Internuclear distances between the metal ion and atoms of the 3'5'-thymidine diphosphate nucleotide were determined from these data by using the Solomon-Bloembergen equation. In general, these distances corresponded closely to those determined by previous X-ray crystallography of the thymidine diphosphate complex. These internuclear distances were also used with a computer program and graphics display to solve for metal : nucleotide geometries which were consistent with the experimental data. A geometry similar to the structure of the metal : nucleotide complex bound to nuclease determined by X-ray analysis was one of the solutions to this computer modeling process. For staphylococcal nuclease the NMR and X-ray methods yield compatible high resolution information about the structure of the active site.

subject areas

  • Animals
  • Binding Sites
  • Calcium
  • Cattle
  • Gadolinium
  • Histidine
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Micrococcal Nuclease
  • Neurophysins
  • Oxytocin
  • Pancreas
  • Phenylalanine
  • Protein Binding
  • Ribonucleases
  • Structure-Activity Relationship
  • Temperature
  • Thymine Nucleotides
  • Tyrosine
  • Vasopressins
  • X-Ray Diffraction
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0300-9084

Digital Object Identifier (DOI)

  • 10.1016/s0300-9084(75)80332-4

PubMed ID

  • 1148335
scroll to property group menus

Additional Document Info

start page

  • 453

end page

  • 460

volume

  • 57

issue

  • 4

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support