Evidence of conformational changes in adsorbed lysozyme molecule on silver colloids

被引：37

作者：

Chandra, Goutam ^{[1
]}

Ghosh, Kalyan S. ^{[2
]}

Dasgupta, Swagata ^{[2
]}

Roy, Anushree ^{[1
]}

机构：

[1] Indian Inst Technol, Dept Phys, Kharagpur 721302, W Bengal, India

[2] Indian Inst Technol, Dept Chem, Kharagpur 721302, W Bengal, India

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2010年 / 47卷 / 03期

关键词：

Lysozyme; Ag colloids; SERS; ENHANCED RAMAN-SPECTROSCOPY; PROTEIN-METAL INTERACTIONS; EGG-WHITE LYSOZYME; AMINO-ACIDS; VIBRATIONAL ANALYSIS; HYDRATED MEDIA; SHORT PEPTIDES; BIOMOLECULES; SCATTERING; REPEATS;

D O I：

10.1016/j.ijbiomac.2010.05.020

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In this article, we discuss metal-protein interactions in the Ag-lysozyme complex by spectroscopic measurements. The analysis of the variation in relative intensities of SERS bands reveals the orientation and the change in conformation of the protein molecules on the Ag surface with time. The interaction kinetics of metal-protein complexes has been analyzed over a period of 3 h via Raman measurements. Our analysis indicates that the Ag nanoparticles most likely interact with Trp123 which is in close proximity to Phe34 of the lysozyme molecule. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：361 / 365

页数：5

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