Evidence map›Paper›PMID 40473898›Full record

ArticleMolecular biotechnology2026

Crystal Structure of Camel (Camelus dromedarius) Methemoglobin: A High Oxygen Affinity Lowland Species.

Balasubramanian Moovarkumudalvan, Sathya Moorthy Ponnuraj, Ramya Ramadoss, Thenmozhi Muthurajan, M N Ponnuswamy

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Article in Molecular biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Balasubramanian Moovarkumudalvan *Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, 600 025, India. bmoovarkumudalvan@gmail.com.ORCID http://orcid.org/0000-0003-1140-883X
Sathya Moorthy Ponnuraj *Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, 600 025, India. sathyamoorthy.pon@tnau.ac.in.
Ramya RamadossMahatma Gandhi Medical Advanced Research Institute (MGMARI), Sri Balaji Vidyapeeth (Deemed to be University), Pondicherry, 607402, India.
Thenmozhi MuthurajanCentre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, 600 025, India.
M N PonnuswamyCentre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, 600 025, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hemoglobin (Hb) is an important oxygen carrying protein inherent in erythrocytes facilitates exchange of oxygen and carbon dioxide from body tissues. Bioengineered synthetic erythrocytes with enhanced Hb proteins have been developed as efficient blood transfusion substitutes to supply oxygen to patients in extreme situations. This has driven research towards the molecular characterization and structural elucidation of Hb in organisms thriving in extreme conditions. Camel is recognized as a typical organism to investigate molecular level adaptations to surpass extreme ecological conditions in the arid zone. The molecular architecture of Hb is linked to the oxygen requirements of an organism to sustain at extreme living conditions. Molecular structure of camel Hb can be determined by X-ray crystallography. In this study, camel Hb is purified and crystallized in the monoclinic space group P2

Indexed as

CamelusMethemoglobinOxygenAnimalsCrystallography, X-RayHumansModels, MolecularProtein ConformationMethemoglobinOxygenCamel hemoglobinCamelid familyHigh oxygen affinityRelaxed state hemoglobin

Identifiers

PMID40473898

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.