Malleable conformation of the elastic PEVK segment of titin: Non-co-operative interconversion of polyproline II helix, β-turn and unordered structures

Kan Ma, Kuan Wang

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

To understand the structural basis of molecular elasticity and protein interaction of the elastic PEVK (Pro-Glu-Val-Lys) segment of the giant muscle protein titin, we carried out a detailed analysis of a representative PEVK module and a 16-module PEVK protein under various environmental conditions. Three conformational states, polyproline II (PPII) helix, β-turn and unordered coil were identified by CD and NMR. These motifs interconvert without long-range co-operativity. As a general trend, the relative content of PPII increases with lower temperature and higher polarity, β-turn increases with lower temperature and lower polarity, and unordered coil increases with higher temperature and higher polarity. NMR studies demonstrate that trans-proline residues are the predominant form at room temperature (22°C), with little trans-to-cis isomerization below 35°C. Ionic strength affects salt bridges between charged side chains, but not the backbone conformation. We conclude that titin PEVK conformation is malleable and responds to subtle environmental changes without co-operativity. This gradual conformational transition may represent a regulatory mechanism for fine-tuning protein interactions and elasticity.

Original languageEnglish
Pages (from-to)687-695
Number of pages9
JournalBiochemical Journal
Volume374
Issue number3
DOIs
Publication statusPublished - Sep 15 2003
Externally publishedYes

Keywords

  • Circular dichroism (CD)
  • Elastic protein
  • Nuclear magnetic resonance (NMR)
  • Polyproline II helix-coil (PhC) motif
  • Titin
  • Trans-to-cis-proline isomerization

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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