UV resonance Raman finds peptide bond-Arg side chain electronic interactions.
UV resonance Raman finds peptide bond-Arg side chain electronic interactions.
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DOI：
10.1021/jp112174s
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发表时间：
2011-05-12
影响因子：
3.3
通讯作者：
Asher, Sanford A.
中科院分区：
文献类型：
--
作者：
Sharma, Bhavya;Asher, Sanford A.
我们测量了氨基酸单体的精氨酸（Arg）振动的紫外共振拉曼激发谱和拉曼退极化比，以及21个残基的丙氨酸肽AAAAA(AAARA)3A （AP）中的Arg在194 ~ 218 nm之间的振动。π→π*肽键内的电子跃迁激发导致UVRR光谱以酰胺肽键振动为主。拉曼截面和激发谱表明，Arg侧链的电子跃迁与AP肽键的电子跃迁混合在一起。AP中的Arg拉曼带表现出与AP中酰胺带相似的拉曼激发谱，具有构象特异性。这些精氨酸激发曲线与精氨酸单体明显不同。Arg在单体溶液中的拉曼退极化比很简单，ρ=0.33表示单电子跃迁增强。相反，我们在AP中看到非常复杂的Arg退极化比，这表明Arg残基被多个电子跃迁共振增强。
We measured the UV resonance Raman excitation profiles and Raman depolarization ratios of the arginine (Arg) vibrations of the amino acid monomer, as well as, Arg in the 21-residue predominantly alanine peptide, AAAAA(AAARA)3A (AP) between 194 and 218 nm. Excitation within the π→π* peptide bond electronic transitions result in UVRR spectra dominated by amide peptide bond vibrations. The Raman cross sections and excitation profiles indicate that the Arg side chain electronic transitions mix with the AP peptide bond electronic transitions. The Arg Raman bands in AP exhibit Raman excitation profiles similar to those of the amide bands in AP which is conformation specific. These Arg excitation profiles distinctly differ from the Arg monomer. The Raman depolarization ratio of Arg in monomeric solution are quite simple with ρ=0.33 indicating enhancement by a single electronic transition. In contrast, we see very complex depolarization ratios of Arg in AP that indicate that the Arg residues are resonance enhanced by multiple electronic transitions.
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DOI：
10.1021/jz900117u
发表时间：
2010-11-30
期刊：
The journal of physical chemistry letters
影响因子：
--
作者：
Bykov SV;Asher SA
通讯作者：
Asher SA
影响因子：
4.4
作者：
DUDIK, JM;JOHNSON, CR;ASHER, SA
通讯作者：
ASHER, SA
影响因子：
2.5
作者：
HILDEBRANDT, P;CZERNUSZEWICZ, RS;SPIRO, TG
通讯作者：
SPIRO, TG
影响因子：
2.5
作者：
Lima, RJC;Freire, PTC;Mendes, J
通讯作者：
Mendes, J
影响因子：
3.5
作者：
LUDWIG, M;ASHER, SA
通讯作者：
ASHER, SA