Progress in Physics

Table of Content

12 October 2020, Volume 38 Issue 3 Next Issue

For Selected:

Download Citations
EndNote Ris BibTeX

Toggle Thumbnails

Weyl Semi-metals and Their Related Transport Properties

2018, 38 (3): 101-131.

PDF (19894KB) ( 516 )

Analogue to graphene and topological insulators, Weyl semimetals become one of the focuses of the condensed matter research recently. Due to their unique gapless bulk states and Fermi arc surface states, Weyl semimetals manifest lots of exotic properties, such as chiral anomaly, chiral magnetic effect, weak anti-localization, chiral Landau-Level, negative magnetoresistance effect and etc. Since impurities and defects inevitably exist in real samples, the study of disorder effects in Weyl semimetals are necessary. In this paper, disorder induced phase transition in both type I and type II Weyl semimetals are reviewed and their global phase diagrams are obtained. These studies enrich the physical understanding of topological Anderson insulator and metal-insulator transition. We also review the influences of both long range and short range disorder on Weyl semimetals. Specially,we find the Boltzmann transport theory is not applicable in some cases. Then, the studies of Imbert-Fedorov shift in Weyl semimetal are reviewed. Finally, we give an explanation about the ultra-high carrier mobility ofWeyl semimetal by combination of wave packet scattering theory and Imbert-Fedorov shift.

Related Articles | Metrics

Molecular Structure and Dynamics of Interfacial Protein Molecules Investigated by Sum Frequency Generation Vibrational Spectroscopy

Wei Feng, Tan Jun-Jun, Zhang Jia-Hui, Li Chuan-Zhao, Wang Wen-Ting, Luo Yi, Ye Shu-Ji

2018, 38 (3): 132-145.

PDF (13483KB) ( 296 )

The interaction of proteins and the interface is a universal but complex phenomenon in nature, which plays an extremely important role in many fields such as physics, biotechnology, chemical engineering, medicine, and environmental science. For example, the structural mutation and dysfunction caused by the misfolding of proteins at the biointerface are directly related to the occurrence and development of various diseases. Precise characterization of the conformations and dynamics of interfacial proteins in situ and in real-time is the core of revealing the function of interfacial proteins, which is of great importance to elucidate the mechanism of neurodegenerative diseases associated with protein aggregation. Nevertheless, there is still a lack of knowledge about their structure and dynamics at this moment. Protein folding is also an unresolved problem in molecule biology central rules. It is mainly because its characterization technology has to require enough structural and temporal resolution as well as requests for in situ, in real-time, in vivo, and non-invasive measurement, yet few methods can meet all the requirements. Sum frequency generation vibrational spectroscopy (SFG-VS) is a powerful technique that can probe the structure and dynamics of interfacial protein molecules at the molecular level. In this review, the application of SFG-VS in the structure and dynamic characterization of interfacial proteins were introduced in details. By probing different protein backbone vibrational bands of amide I, amide III and amide A in situ and in real-time, the precise measurements of the structure, conformation transition and dynamic features of interfacial protein molecules can be achieved, which can further reveal the molecular mechanisms of protein-membrane interaction, protein-protein interaction and protein aggregation. This review will provide a new train of thought for people to study the physical and chemical problems of complex interface systems.