Raman spectroscopy of proteins: from peptides to large assemblies

被引：378

作者：

Tuma, R ^{[1
]}

机构：

[1] Univ Helsinki, Inst Biotechnol, Helsinki 00014, Finland

[2] Univ Helsinki, Dept Biol & Environm Sci, Helsinki 00014, Finland

[3] Univ Helsinki, Inst Biotechnol, Helsinki 00014, Finland

来源：

JOURNAL OF RAMAN SPECTROSCOPY | 2005年 / 36卷 / 04期

关键词：

protein folding; peptides; amide modes; enzyme-substrate interaction; Raman difference spectroscopy;

D O I：

10.1002/jrs.1323

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

Raman spectroscopy has become a versatile tool in protein science and biotechnology. Recent advances in spectral assignments and vibrational theory, examples of use in structural biology and selected industrial applications are discussed. New insights into protein folding, assembly and aggregation were obtained by classical Raman spectroscopy. Raman spectroscopy has been used to characterize intrinsically unstructured proteins. The improved instrument sensitivity made it possible to use Raman difference spectroscopy to characterize enzyme-substrate interactions. Specifically, Raman crystallography has been instrumental in the delineation of protein-ligand interactions with a resolution surpassing that of x-ray diffraction. Numerous applications of Raman spectroscopy to protein analysis in biotechnology and food industry have been facilitated by the new generation of commercial Raman instruments. Copyright (c) 2005 John Wiley & Sons, Ltd.

引用

页码：307 / 319

页数：15

共 136 条

[61] Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation [J].

Mancini, EJ ;

Kainov, DE ;

Grimes, JM ;

Tuma, R ;

Bamford, DH ;

Stuart, DI .

CELL, 2004, 118 (06) :743-755

[62] Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes [J].

Miura, T ;

Suzuki, K ;

Kohata, N ;

Takeuchi, H .

BIOCHEMISTRY, 2000, 39 (23) :7024-7031

[63]

Miura T, 1995, Subcell Biochem, V24, P55

[64] Copper selectively triggers β-sheet assembly of an N-terminally truncated amyloid β-peptide beginning with Glu3 [J].

Miura, T ;

Mitani, S ;

Takanashi, C ;

Mochizuki, N .

JOURNAL OF INORGANIC BIOCHEMISTRY, 2004, 98 (01) :10-14

[65]

Miura T, 1998, J RAMAN SPECTROSC, V29, P41, DOI 10.1002/(SICI)1097-4555(199801)29:1<41::AID-JRS212>3.0.CO

[66]

2-R

[67] Binding of iron(III) to the single tyrosine residue of amyloid β-peptide probed by Raman spectroscopy [J].

Miura, T ;

Suzuki, K ;

Takeuchi, H .

JOURNAL OF MOLECULAR STRUCTURE, 2001, 598 (01) :79-84

[68] Binding mode of Congo Red to Alzheimer's amyloid β-peptide studied by UV Raman spectroscopy [J].

Miura, T ;

Yamamiya, C ;

Sasaki, M ;

Suzuki, K ;

Takeuchi, H .

JOURNAL OF RAMAN SPECTROSCOPY, 2002, 33 (07) :530-535

[69] PERTURBATION TREATMENT OF THE CHARACTERISTIC VIBRATIONS OF POLYPEPTIDE CHAINS IN VARIOUS CONFIGURATIONS [J].

MIYAZAWA, T .

JOURNAL OF CHEMICAL PHYSICS, 1960, 32 (06) :1647-1652

[70] Amide modes of the α-helix:: Raman spectroscopy of filamentous virus fd containing peptide 13C and 2H labels in coat protein subunits [J].

Overman, SA ;

Thomas, GJ .

BIOCHEMISTRY, 1998, 37 (16) :5654-5665

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