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

作　　者：N.Meenakshisundaram Kamatchi Sankaranarayanan 

机构地区：[1]Centre for Nonlinear Science and Engineering,School of Electrical and Electronics Engineering,SASTRA University [2]DST-INSPIRE Faculty,Department of Energy and Environment,National Institute of Technology

出　　处：《光谱学与光谱分析》2016年第5期1629-1633,共5页Spectroscopy and Spectral Analysis

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.

关 键 词：Protein folding Molecular crowders Interfacial viscosity Fluorescent probes 

分 类 号：O657.3[理学—分析化学]