Fermi resonance as a means to determine the hydrogen-bonding status of two infrared probes
Author:
Affiliation:
1. Department of Chemistry
2. University of Pennsylvania
3. Philadelphia
4. USA
5. Ultrafast Optical Processes Laboratory, University of Pennsylvania
6. Department of Physics
7. Beijing Normal University
Abstract
This study shows that the Fermi resonance coupling constant (W) is indicative of the hydrogen-bonding status of a CO or CN functional group.
Funder
National Institute of General Medical Sciences
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP02442H
Reference36 articles.
1. Site-Specific Infrared Probes of Proteins
2. Transparent Window Vibrational Probes for the Characterization of Proteins With High Structural and Temporal Resolution
3. Vibrational Probes: From Small Molecule Solvatochromism Theory and Experiments to Applications in Complex Systems
4. Using Nitrile-Derivatized Amino Acids as Infrared Probes of Local Environment
5. Site-Specific Conversion of Cysteine Thiols into Thiocyanate Creates an IR Probe for Electric Fields in Proteins
Cited by 40 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Fermi Resonance of the N-D Stretching Mode Probing the Local Hydrogen-Bonding Environment in Proteins;The Journal of Physical Chemistry B;2024-06-05
2. Investigating local field tuning Fermi resonance of CS2 by Raman spectroscopy and DFT calculations;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2024-04
3. Elucidating state-specific dynamics of 1La and 1Lb in cyanoindole derivatives using UV/Vis pump IR detection;Chemical Physics;2024-01
4. Autocatalysis in Eschenmoser Coupling Reactions;Chemistry – A European Journal;2023-12-21
5. Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy;The Journal of Chemical Physics;2023-10-23
1.学者识别学者识别
2.学术分析学术分析
3.人才评估人才评估
"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370
www.globalauthorid.com
TOP
Copyright © 2019-2024 北京同舟云网络信息技术有限公司 京公网安备11010802033243号 京ICP备18003416号-3