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利用紫外和可见共振拉曼光谱深入了解蛋白质结构与动力学

Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.

作者信息

López-Peña Ignacio, Leigh Brian S, Schlamadinger Diana E, Kim Judy E

机构信息

Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92093, United States.

出版信息

Biochemistry. 2015 Aug 11;54(31):4770-83. doi: 10.1021/acs.biochem.5b00514. Epub 2015 Jul 29.

DOI:10.1021/acs.biochem.5b00514
PMID:26219819
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5092233/
Abstract

Raman spectroscopy is a form of vibrational spectroscopy based on inelastic scattering of light. In resonance Raman spectroscopy, the wavelength of the incident light falls within an absorption band of a chromophore, and this overlap of excitation and absorption energy greatly enhances the Raman scattering efficiency of the absorbing species. The ability to probe vibrational spectra of select chromophores within a complex mixture of molecules makes resonance Raman spectroscopy an excellent tool for studies of biomolecules. In this Current Topic, we discuss the type of molecular insights obtained from steady-state and time-resolved resonance Raman studies of a prototypical photoactive protein, rhodopsin. We also review recent efforts in ultraviolet resonance Raman investigations of soluble and membrane-associated biomolecules, including integral membrane proteins and antimicrobial peptides. These examples illustrate that resonance Raman is a sensitive, selective, and practical method for studying the structures of biological molecules, and the molecular bonding, geometry, and environments of protein cofactors, the backbone, and side chains.

摘要

拉曼光谱是一种基于光的非弹性散射的振动光谱形式。在共振拉曼光谱中,入射光的波长落在发色团的吸收带内,这种激发和吸收能量的重叠极大地提高了吸收物种的拉曼散射效率。能够探测复杂分子混合物中特定发色团的振动光谱,使得共振拉曼光谱成为研究生物分子的出色工具。在本专题中,我们讨论了从对典型光活性蛋白视紫红质的稳态和时间分辨共振拉曼研究中获得的分子见解类型。我们还回顾了近期在紫外共振拉曼研究可溶性和膜相关生物分子方面所做的努力,包括整合膜蛋白和抗菌肽。这些例子表明,共振拉曼是研究生物分子结构以及蛋白质辅因子、主链和侧链的分子键合、几何结构和环境的一种灵敏、选择性强且实用的方法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/bfc371f8937e/nihms823845f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/e52260656baa/nihms823845f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/f8a04771bcae/nihms823845f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/c3109a5d05bf/nihms823845f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/60e2734967c7/nihms823845f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/56e122122c7d/nihms823845f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/bfc371f8937e/nihms823845f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/e52260656baa/nihms823845f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/f8a04771bcae/nihms823845f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/c3109a5d05bf/nihms823845f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/60e2734967c7/nihms823845f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/56e122122c7d/nihms823845f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bfd5/5092233/bfc371f8937e/nihms823845f6.jpg

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Bilayer surface association of the pHLIP peptide promotes extensive backbone desolvation and helically-constrained structures.pHLIP 肽的双层表面缔合促进了广泛的主链去溶剂化和螺旋受限结构。
Biophys Chem. 2014 Mar-Apr;187-188:1-6. doi: 10.1016/j.bpc.2013.12.004. Epub 2013 Dec 28.
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Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.
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The degree of doneness affected molecular changes and protein digestibility of pork.熟度影响猪肉的分子变化和蛋白质消化率。
Front Nutr. 2023 Jan 4;9:1084779. doi: 10.3389/fnut.2022.1084779. eCollection 2022.
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