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National Institute of Allergy and Infectious Disease
NIH 3D
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A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN

https://doi.org/10.60705/3dpx/16912.3
NIH 3D Model Entry
3DPX-016912
How to Cite
NIH 3D. (2026). A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN (Version 3.x). NIH 3D. https://doi.org/10.60705/3DPX/16912.3
Summary Information

Title: A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN

Description:

Data extracted from PDB 1HDA in the Protein Data Bank was used by NIH 3D's workflows to automatically generate the 3D representations presented in this DOI.

Creator(s):

Contributor(s):

  • NIH 3D, Data Manager

Publisher: NIH 3D

Publication Year: 2026

Version: 3.x

"x" corresponds to any minor version