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Article

The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.

Biophysical journal - 9 May 2017

Sato Satoshi, Cho Jae-Hyun, Peran Ivan, Soydaner-Azeloglu Rengin G, Raleigh Daniel P

Abstract excerpt

The N-terminal domain of L9 (NTL9) is a 56-residue mixed α-β protein that lacks disulfides, does not bind cofactors, and folds reversibly. NTL9 has been widely used as a model system for experimental and computational studies of protein folding and for investigations of the unfolded state. The role of side-chain interactions in the folding of NTL9 is probed by mutational analysis. ϕ-values, which represent the...

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Identifiers

PMID: 28494951
DOI: 10.1016/j.bpj.2017.01.034
PMCID: PMC5425357

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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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The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.PMID 28494951Read ↗

The unfolded state of NTL9 is compact in the absence of denaturant.Semantic proximity Read ↗

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Energetically significant networks of coupled interactions within an unfolded protein.Semantic proximity Read ↗

Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure.Semantic proximity Read ↗

The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures.Semantic proximity Read ↗

Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins.Semantic proximity Read ↗

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