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Article

Role of N-terminal residues on folding and stability of C-phycoerythrin: simulation and urea-induced denaturation studies.

Journal of biomolecular structure & dynamics - 1 Jan 2015

Anwer Khalid, Sonani Ravi, Madamwar Datta, Singh Parvesh, Khan Faez, Bisetty Krishna, Ahmad Faizan, Hassan Md Imtaiyaz

Abstract excerpt

The conformational state of biliproteins can be determined by optical properties of the covalently linked chromophores. Recently determined crystal structure of truncated form of α-subunit of cyanobacterial phycoerythrin (αC-PE) from Phormidium tenue provides a new insight into the structure-function relationship of αC-PE. To compare their stabilities, we have measured urea-induced denaturation transitions of the...

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PMID: 24279700
DOI: 10.1080/07391102.2013.855144

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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