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Article

Modification of axial fiber contact residues impact sickle hemoglobin polymerization by perturbing a network of coupled interactions.

The protein journal - 1 Oct 2007

Banerjee Srijita, Mirsamadi Neda, Anantharaman Lavanya, Sivaram Mylavarapu V S, Gupta Rasik B, Choudhury Devapriya, Roy Rajendra P

Abstract excerpt

The identity of intermolecular contact residues in sickle hemoglobin (HbS) fiber is largely known. However, our knowledge about combinatorial effects of two or more contact sites or the mechanistic basis of such effects is rather limited. Lys16, His20, and Glu23 of the alpha-chain occur in intra-double strand axial contacts in the sickle hemoglobin (HbS) fiber. Here we have constructed two novel double mutants,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 17514412
DOI: 10.1007/s10930-007-9084-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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