ArticlebioRxiv : the preprint server for biology2026
Characterizing the Conformational Dynamics of an Intrinsically Disordered Localization Sequence.
Article in bioRxiv : the preprint server for biology, 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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4 authors.
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Abstract
Mitochondrial localization peptides (MLPs) play a critical role in directing proteins to mitochondria, yet how subtle sequence variations influence their conformational behavior remains poorly understood. Here, we investigate the conformational dynamics of a 15-residue MLP derived from the androgen receptor, together with a comprehensive panel of single-residue variants generated by systematic substitution at the second position. Across all variants, the peptide remains intrinsically disordered, exhibiting broad conformational heterogeneity and no stable folded state. Global measures of compactness show that single-residue substitutions induce only modest changes to overall peptide dimensions. In contrast, residue-level analysis reveals that the identity of the second residue subtly reshapes local structural preferences, particularly near the N-terminus. Small or hydrophobic substitutions enhance transient
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