Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability

Author:

Ou Xinwen1ORCID,Xue Bin2ORCID,Lao Yichong1ORCID,Wutthinitikornkit Yanee1ORCID,Tian Ranran1ORCID,Zou Aodong1ORCID,Yang Lingyun3ORCID,Wang Wei2ORCID,Cao Yi2ORCID,Li Jingyuan1ORCID

Affiliation:

1. Zhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.

2. Collaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing 210093, China.

3. iHuman Institute, Shanghai Tech University, 393 Hua Xia Zhong Road, Shanghai 201210, China.

Abstract

Aromatic and basic residue form pair in intrinsically disordered adhesive protein, and such pairs dominate protein adsorption.

Funder

National Natural Science Foundation of China

China Postdoctoral Science Foundation

National Natural Science Foundation of Jiangsu Province

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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