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Article

Factors that drive peptide assembly and fibril formation: experimental and theoretical analysis of Sup35 NNQQNY mutants.

The journal of physical chemistry. B - 18 Jul 2013

Do Thanh D, Economou Nicholas J, LaPointe Nichole E, Kincannon William M, Bleiholder Christian, Feinstein Stuart C, Teplow David B, Buratto Steven K, Bowers Michael T

Abstract excerpt

Residue mutations have substantial effects on aggregation kinetics and propensities of amyloid peptides and their aggregate morphologies. Such effects are attributed to conformational transitions accessed by various types of oligomers such as steric zipper or single β-sheet. We have studied the aggregation propensities of six NNQQNY mutants: NVVVVY, NNVVNV, NNVVNY, VIQVVY, NVVQIY, and NVQVVY in water using a...

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Identifiers

PMID: 23802812
DOI: 10.1021/jp4046287

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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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