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Role of Interfacial Viscosity and pH in L-Phenylalanine,L-Tryptophan Molecular Rotors

Role of Interfacial Viscosity and pH in L-Phenylalanine,L-Tryptophan Molecular Rotors
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摘要 Protein folding involves the aminoacid sequence to come forth and form an energy minimized structure.Recently molecular crowding leading to increase in viscosity is said to be one of the major concerns affecting protein folding.Many external fluorescent probes are used to detect such increases in viscosity.Since most of the protein sequences contain L-Phe and L-Trp,in this study we have used these aminoacids as probes to detect changes in viscosity.This study will help to advance the knowledge on molecular crowding effects in protein folding. Protein folding involves the aminoacid sequence to come forth and form an energy minimized structure.Recently molecular crowding leading to increase in viscosity is said to be one of the major concerns affecting protein folding.Many external fluorescent probes are used to detect such increases in viscosity.Since most of the protein sequences contain L-Phe and L-Trp,in this study we have used these aminoacids as probes to detect changes in viscosity.This study will help to advance the knowledge on molecular crowding effects in protein folding.
出处 《光谱学与光谱分析》 SCIE EI CAS CSCD 北大核心 2016年第5期1629-1633,共5页 Spectroscopy and Spectral Analysis
关键词 Protein folding Molecular crowders Interfacial viscosity Fluorescent probes Protein folding Molecular crowders Interfacial viscosity Fluorescent probes
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参考文献13

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