The discovery of 212Hbs as short haemoproteins structurally related to haemo- globins, in the 1990s, was complemented by extensive sequence and crystallo- graphic investigations in the early 2000s. Amino acid sequences first provided a clear indication that the 2/2Hb family (formerly known as "truncated Hbs") is composed of three main protein groups (I, II and III) that display low pri- mary structure conservation relative to vertebrate Hbs. Crystal structures showed that a simple protein fold, essentially composed of four
A Crystallographer's Perspective on the 2/2Hb Family
Mario Milani;Marco Nardini;Martino Bolognesi
2008
Abstract
The discovery of 212Hbs as short haemoproteins structurally related to haemo- globins, in the 1990s, was complemented by extensive sequence and crystallo- graphic investigations in the early 2000s. Amino acid sequences first provided a clear indication that the 2/2Hb family (formerly known as "truncated Hbs") is composed of three main protein groups (I, II and III) that display low pri- mary structure conservation relative to vertebrate Hbs. Crystal structures showed that a simple protein fold, essentially composed of fourFile in questo prodotto:
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