Abstract

Metastable β titanium alloys with both twinning (TWIP) and martensite transformation (TRIP) usually exhibit a low yield strength of between 200 and 500 MPa, but high strain hardening rate and large uniform elongation. Alloys that exhibit twinning on a single system provide a higher yield strength, but a lower strain hardening rate. Here, for the first time, we report a new alloy (Ti-7Mo-3Cr wt%) with both high yield strength (695 MPa) and high work hardening rate (∼1900 MPa) and a substantial 33.3% uniform elongation. The deformation mechanisms were systematically investigated using EBSD and TEM for samples strained to 1.3%, 5% and 16%. The high yield strength was achieved through initial deformation mechanisms of two twin systems, namely both {332}<113> and {112}<111> twinning. Importantly, the martensite transformation was suppressed at this stage of deformation. The combination of two twin systems, with approximately the same intensity, resulted in a high strain hardening rate (1600 MPa–1900 MPa), much greater compared to alloys that exhibit a single twin system. Moreover, the TRIP effect was observed at strains greater than 5%, which also contributed to the high strain hardening rate large uniform elongation.

Highlights

  • Smc/kleisin complexes facilitate chromosome segregation in bacteria as well as eukaryotes (Schleiffer et al, 2003)

  • We found that co-entrapment of sister DNAs within cohesin rings invariably accompanies sister chromatid cohesion

  • Organization of DNA into Chromatid-like Threads Does Not Require Entrapment of DNA by Cohesin Rings We addressed whether smc1DDsmc3AAA cohesin is still active in organizing chromosome topology

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Summary

Introduction

Smc/kleisin complexes facilitate chromosome segregation in bacteria as well as eukaryotes (Schleiffer et al, 2003) The latter have three types: condensin, cohesin, and the Smc5/6 complex (Haering and Gruber, 2016). Smc and Smc are rod-shaped proteins containing 50-nmlong intra-molecular anti-parallel coiled coils with a hinge/dimerization domain at one end and an ABC-like ATPase head domain composed of the protein’s N- and C-terminal sequences at the other. They bind each other via their hinges to form V-shaped heterodimers whose apical ATPases are interconnected by a single Scc polypeptide (Gruber et al, 2003). Bacterial Smc/kleisin complexes form similar structures, suggesting that asymmetric ring formation is a universal feature (Burmann et al, 2013)

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