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Article

1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin.

European journal of biochemistry - 15 Dec 1992

Alexandrescu A T, Broadhurst R W, Wormald C, Chyan C L, Baum J, Dobson C M

Abstract excerpt

1H-NMR assignments have been defined for the aromatic-ring protons of the bovine, guinea pig and human variants of alpha-lactalbumin. Spin-system networks were identified by means of double-quantum-filtered two-dimensional J-correlated spectroscopy and two-dimensional relayed coherence spectroscopy data. Analysis of two-dimensional nuclear-Overhauser-enhancement spectroscopy data of the proteins indicated that in...

Topics

Amino Acid Sequence
Animals
Cattle
Genetic Variation
Guinea Pigs
Histidine
Humans
Hydrogen
Lactalbumin
Magnetic Resonance Spectroscopy
Muramidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Source

Identifiers

PMID: 1483454
DOI: 10.1111/j.1432-1033.1992.tb17471.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1483454-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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