Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of beta-sheet structures

被引:89
作者
Marsh, D
机构
[1] Max-Planck-Inst. Biophysik. Chem., Abteilung Spektroskopie
[2] Max-Planck-Inst. Biophysik. Chem., Abteilung 010 Spektroskopie, D-37077 Göttingen-Nikolausberg, Am Fassberg
关键词
D O I
10.1016/S0006-3495(97)78914-8
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The transition moments for the amide bands from beta-sheet peptide structures generally do not exhibit axial symmetry about the director in linearly polarized Fourier transform infrared (FTIR) measurements on oriented systems. The angular dependences of the dichroic ratios of the amide bands are derived for beta-sheet structures in attenuated total reflection (ATR) and polarized transmission experiments on samples that are oriented with respect to the normal to the substrate and are randomly distributed with respect to the azimuthal angle in the plane of the orienting substrate. The orientational distributions of both the beta-strands and the beta-sheets are considered, and explicit expressions are given for the dichroic ratios of the amide I and amide II bands. The dichroic ratio of the amide II band, which is parallel polarized, can yield the orientation of the beta-strands directly, but to specify the orientations of the beta-sheets completely requires measurement of the dichroic ratios of both the amide I and amide II bands, or generally two bands with parallel and perpendicular polarizations. A random distribution in lilt of the planes of the beta-sheets does not give rise to equal dichroic ratios for bands with perpendicular and parallel polarizations, such as the amide and amide II bands. The results are applied to previous ATR and polarized transmission FTIR measurements on a potassium channel-associated peptide, the Escherichia coli outer membrane protein OmpA, and the E. coli OmpF porin protein in oriented membranes.
引用
收藏
页码:2710 / 2718
页数:9
相关论文
共 34 条
[11]   ORIENTATION OF MELITTIN IN PHOSPHOLIPID-BILAYERS - A POLARIZED ATTENUATED TOTAL REFLECTION INFRARED STUDY [J].
FREY, S ;
TAMM, LK .
BIOPHYSICAL JOURNAL, 1991, 60 (04) :922-930
[12]   SECONDARY STRUCTURE AND DOSAGE OF SOLUBLE AND MEMBRANE-PROTEINS BY ATTENUATED TOTAL REFLECTION FOURIER-TRANSFORM INFRARED-SPECTROSCOPY ON HYDRATED FILMS [J].
GOORMAGHTIGH, E ;
CABIAUX, V ;
RUYSSCHAERT, JM .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1990, 193 (02) :409-420
[13]   THE TRANSMEMBRANE DOMAINS OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR CONTAIN ALPHA-HELICAL AND BETA-STRUCTURES [J].
GORNETSCHELNOKOW, U ;
STRECKER, A ;
KADUK, C ;
NAUMANN, D ;
HUCHO, F .
EMBO JOURNAL, 1994, 13 (02) :338-341
[14]  
Harrick N.J., 1967, INTERNAL REFLECTION
[15]  
HORVATH LI, 1995, BIOCHEMISTRY-US, V34, P3964
[16]   VIBRATIONAL SPECTROSCOPY AND CONFORMATION OF PEPTIDES, POLYPEPTIDES, AND PROTEINS [J].
KRIMM, S ;
BANDEKAR, J .
ADVANCES IN PROTEIN CHEMISTRY, 1986, 38 :181-364
[17]   INTERMOLECULAR INTERACTION EFFECTS IN AMIDE I VIBRATIONS OF BETA POLYPEPTIDES [J].
KRIMM, S ;
ABE, Y .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1972, 69 (10) :2788-2792
[18]  
MANNELLA CA, 1992, J BIOENERG BIOMEMBR, V24, P7, DOI 10.1007/BF00769525
[19]   Peptide models for membrane channels [J].
Marsh, D .
BIOCHEMICAL JOURNAL, 1996, 315 :345-361