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Article

Proton NMR studies of transforming and nontransforming H-ras p21 mutants.

Biochemistry - 16 Jan 1990

Schlichting I, John J, Frech M, Chardin P, Wittinghofer A, Zimmermann H, Rösch P

Abstract excerpt

One- and two-dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site-directed mutagenesis were used to study the influence of mutations on the conformation of the H-ras oncogene product p21. No severe structural differences between the different mutants, whether they were transforming or nontransforming, could be detected. Initially, selective incorporation of 3,5-deuterated tyrosyl residues...

Topics

Base Sequence
Cell Transformation, Neoplastic
DNA
Guanosine Diphosphate
Guanosine Triphosphate
Magnesium
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutation
Oncogene Protein p21(ras)
Phenylalanine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Tyrosine

Source

Identifiers

PMID: 2405906
DOI: 10.1021/bi00454a026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2405906-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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