Peng Xiao

ORCID: 0000-0002-6430-0278
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About
Contact & Profiles
Research Areas
  • Advanced NMR Techniques and Applications
  • Protein Structure and Dynamics
  • Lipid Membrane Structure and Behavior
  • Anesthesia and Neurotoxicity Research
  • Biofuel production and bioconversion
  • Metallic Glasses and Amorphous Alloys
  • Lignin and Wood Chemistry
  • Traumatic Brain Injury and Neurovascular Disturbances
  • Neurological Disease Mechanisms and Treatments
  • Quantum, superfluid, helium dynamics
  • RNA and protein synthesis mechanisms
  • Polysaccharides and Plant Cell Walls
  • Theoretical and Computational Physics
  • Spectroscopy and Quantum Chemical Studies
  • nanoparticles nucleation surface interactions

University of Guelph
2019-2024

Fujian Provincial Hospital
2019

Fujian Medical University
2019

Lignification waterproofs and strengthens the secondary plant cell wall, while increasing energy cost associated with releasing sugars for biofuel production. The physical association between lignin carbohydrate scaffold that accommodates polymerization, as well temporally distinct roles of different units partners during lignification, remain largely unclear. Here we map lignin-carbohydrate interactions by solid-state NMR in 13C-labeled Arabidopsis inflorescence stems walls are formed....

10.1101/2025.01.27.635099 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2025-01-28

The plant cell wall, a highly abundant renewable resource, remains insufficiently understood in terms of its structure, particularly the architecture cellulose microfibrils and their interactions with hemicellulose lignin, which impede development efficient downstream conversion. Here we present an alternative model xylan-bound microfibril wall intact wheat straw, using solid-state nuclear magnetic resonance (ssNMR) coupled X-ray scattering techniques. We show that spectroscopic data can be...

10.1101/2025.03.11.642666 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2025-03-14

Abstract Membrane protein folding, structure, and function strongly depend on a cell membrane environment, yet detailed characterization of folding within lipid bilayer is challenging. Studies reversible unfolding yield valuable information the energetics hierarchy interactions contributing to stability. Here, we devise methodology that combines hydrogen-deuterium (H/D) exchange solid-state NMR (SSNMR) follow in membranes at atomic resolution through detecting changes water-accessible...

10.1038/s41467-019-11849-8 article EN cc-by Nature Communications 2019-08-27

Understanding how the amino acid sequence dictates protein structure and defines its stability is a fundamental problem in molecular biology. It especially challenging for membrane proteins that reside complex environment of lipid bilayer. Here, we obtain an atomic-level picture thermally induced unfolding membrane-embedded α-helical protein, human aquaporin 1, using solid-state nuclear magnetic resonance spectroscopy. Our data reveal hierarchical two-step pathway begins with structured...

10.1126/sciadv.adm7907 article EN cc-by-nc Science Advances 2024-05-17

Objective To investigate the mechanism of cerebral protection by treatment butylphthalide (NBP) and its effect to mitochondria in a porcine model cardiac arrest (CA) after cardiopulmonary resuscitation (CPR). Methods Healthy Wuzhishan pigs weighting (30±2) kg were divide into three groups randomly(random number): The sham group (n=6), control (n=12) NBP (n=12). Operation was performed group. Cardiac ventricular fibrillation induced programed electrical stimulation After CPR,...

10.3760/cma.j.issn.1671-0282.2019.08.011 article EN 2019-08-10
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