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Article

Role of Leu-beta 88 in the hydrophobic acceptor pocket for Val-beta 6 during hemoglobin S polymerization.

The Journal of biological chemistry - 1 Jul 1994

Adachi K, Konitzer P, Paulraj C G, Surrey S

Abstract excerpt

X-ray crystallographic studies indicate that the hydrophobic acceptor pocket made by E and F helices involving Leu-beta 88 and Phe-beta 85 is critical for the formation of stable hydrophobic interactions with Val-beta 6 on an adjacent deoxy-hemoglobin (Hb) S tetramer. Ala and Phe substitutions at the beta 88 position in Hb S were made using a yeast expression system in an effort to clarify the role of Leu-beta 88...

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PMID: 8021253

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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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