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Article

Effect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMR.

PloS one - 1 Jan 2016

Konagaya Yuta, Miyakawa Rina, Sato Masumi, Matsugami Akimasa, Watanabe Satoru, Hayashi Fumiaki, Kigawa Takanori, Nishimura Chiaki

Abstract excerpt

To test the existence of the salt bridge and stability of the HIV-1 p17 matrix protein, an E12A (mutated at helix 1) was established to abolish possible electrostatic interactions. The chemical shift perturbation from the comparison between wild type and E12A suggested the existence of an electrostatic interaction in wild type between E12 and H89 (located in helix 4). Unexpectedly, the studies using urea...

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Identifiers

PMID: 27907055
DOI: 10.1371/journal.pone.0167176
PMCID: PMC5132258

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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