Raman crystallography and other biochemical applications of Raman microscopy

被引:87
作者
Carey, Paul R. [1 ]
机构
[1] Case Western Reserve Univ, Dept Biochem, Cleveland, OH 44106 USA
关键词
transcarboxylase; drug screening; beta-lactamase; amyloid A beta; alpha-synuclein;
D O I
10.1146/annurev.physchem.57.032905.104521
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Recent Studies using, a Raman microscope have shown that single protein crystals provide an ideal platform to undertake Raman difference spectroscopic analyses under nonresonance conditions. This approach, termed Raman crystallography. provides a means of characterizing chemical events within the crystal such as ligand binding and enzyme reactions. In many cases Raman crystallography goes hand in hand with X-ray crystallographic studies because the Raman results call inform the X-ray crystallographer about the status of chemical events in the crystal prior to flash freezing and X-ray analysis. In turn, the combined data from the Raman and X-ray analyses are highly synergistic and offer novel perspectives on structure and dynamics in enzyme active sites. In a related area, protein misfolding, Raman microscopy can provide detailed insights into the chemistry of the amyloid plaques associated with Alzheimer's disease and into the intermediates oil the alpha-synuclein protein misfolding pathway implicated in Parkinson's disease.
引用
收藏
页码:527 / 554
页数:28
相关论文
共 42 条
[1]   Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy [J].
Altose, MD ;
Zheng, YG ;
Dong, J ;
Palfey, BA ;
Carey, PR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (06) :3006-3011
[2]   Secondary structure of α-synuclein oligomers:: Characterization by Raman and atomic force microscopy [J].
Apetri, MM ;
Maiti, NC ;
Zagorski, MG ;
Carey, PR ;
Anderson, VE .
JOURNAL OF MOLECULAR BIOLOGY, 2006, 355 (01) :63-71
[3]   Senile plaque composition and posttranslational modification of amyloid-β peptide and associated proteins [J].
Atwood, CS ;
Martins, RN ;
Smith, MA ;
Perry, G .
PEPTIDES, 2002, 23 (07) :1343-1350
[4]   Raman spectroscopy of the Ff gene V protein and complexes with poly(dA): Nonspecific DNA recognition and binding [J].
Benevides, JM ;
Terwilliger, TC ;
Vohnik, S ;
Thomas, GJ .
BIOCHEMISTRY, 1996, 35 (29) :9603-9609
[5]   Following ligand binding and ligand reactions in proteins via Raman crystallography [J].
Carey, PR ;
Dong, J .
BIOCHEMISTRY, 2004, 43 (28) :8885-8893
[6]   RESONANCE RAMAN SPECTROSCOPIC STUDIES OF 2,4-DINITROPHENYL HAPTEN-ANTIBODY INTERACTIONS [J].
CAREY, PR ;
FROESE, A ;
SCHNEIDER, H .
BIOCHEMISTRY, 1973, 12 (12) :2198-2208
[7]   Raman spectroscopy, the sleeping giant in structural biology, awakes [J].
Carey, PR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (38) :26625-26628
[8]   UNLOCKING THE SECRETS OF ENZYME POWER USING RAMAN-SPECTROSCOPY [J].
CAREY, PR ;
TONGE, PJ .
ACCOUNTS OF CHEMICAL RESEARCH, 1995, 28 (01) :8-13
[9]   Coherent anti-Stokes Raman scattering microscopy: Instrumentation, theory, and applications [J].
Cheng, JX ;
Xie, XS .
JOURNAL OF PHYSICAL CHEMISTRY B, 2004, 108 (03) :827-840
[10]  
Deng H, 1999, METHOD ENZYMOL, V308, P176