Literature DB >> 2911719

Protein structure determination in solution by nuclear magnetic resonance spectroscopy.

K Wüthrich1.   

Abstract

Knowledge of three-dimensional protein structures is one of the foundations of protein design and protein engineering. Nuclear magnetic resonance spectroscopy was recently introduced as a second method for protein structure determination, in addition to the well-established diffraction techniques with protein single crystals. This new approach enables one to carry out detailed structural studies of proteins in solution and other noncrystalline states, which may be similar or identical to the physiological environment, and promises new insights into the dynamics of protein molecules and the protein-folding problem.

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Year:  1989        PMID: 2911719     DOI: 10.1126/science.2911719

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  35 in total

1.  Simulation of NOESY spectra of DNA segments: a new scaling procedure for iterative comparison of calculated and experimental NOE intensities.

Authors:  R Nibedita; R A Kumar; A Majumdar; R V Hosur
Journal:  J Biomol NMR       Date:  1992-09       Impact factor: 2.835

2.  Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.

Authors:  W Braun; M Vasák; A H Robbins; C D Stout; G Wagner; J H Kägi; K Wüthrich
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-01       Impact factor: 11.205

3.  Solvent dielectric effects on protein dynamics.

Authors:  R Affleck; C A Haynes; D S Clark
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-01       Impact factor: 11.205

Review 4.  Protein folding.

Authors:  T E Creighton
Journal:  Biochem J       Date:  1990-08-15       Impact factor: 3.857

5.  A PDZ domain recapitulates a unifying mechanism for protein folding.

Authors:  Stefano Gianni; Christian D Geierhaas; Nicoletta Calosci; Per Jemth; Geerten W Vuister; Carlo Travaglini-Allocatelli; Michele Vendruscolo; Maurizio Brunori
Journal:  Proc Natl Acad Sci U S A       Date:  2006-12-19       Impact factor: 11.205

6.  Efficient analysis of protein 2D NMR spectra using the software package EASY.

Authors:  C Eccles; P Güntert; M Billeter; K Wüthrich
Journal:  J Biomol NMR       Date:  1991-07       Impact factor: 2.835

7.  Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.

Authors:  P Güntert; K Wüthrich
Journal:  J Biomol NMR       Date:  1991-11       Impact factor: 2.835

8.  Torsion angle approach to nucleic acid distance geometry: TANDY.

Authors:  R A Kumar; R V Hosur; G Govil
Journal:  J Biomol NMR       Date:  1991-11       Impact factor: 2.835

9.  Computer-assisted assignment of 2D 1H NMR spectra of proteins: basic algorithms and application to phoratoxin B.

Authors:  G J Kleywegt; R Boelens; M Cox; M Llinás; R Kaptein
Journal:  J Biomol NMR       Date:  1991-05       Impact factor: 2.835

10.  Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy.

Authors:  K D O'Neal; M V Chari; C H Mcdonald; R G Cook; L Y Yu-Lee; J D Morrisett; W T Shearer
Journal:  Biochem J       Date:  1996-05-01       Impact factor: 3.857

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