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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >Conformation-Specific Spectroscopy of Asparagine-Containing Peptides: Influence of Single and Adjacent Asn Residues on Inherent Conformational Preferences
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Conformation-Specific Spectroscopy of Asparagine-Containing Peptides: Influence of Single and Adjacent Asn Residues on Inherent Conformational Preferences

机译：含天冬氨酸肽的统一特异性光谱：单个和相邻ASN残基对固有构象偏好的影响

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摘要

The infrared and ultraviolet spectra of a series of capped asparagine-containing peptides, Ac-Asn-NHBn, Ac-Ala-Asn-NHBn, and Ac-Asn-Asn-NHBn, have been recorded under jet-cooled conditions in the gas phase in order to probe the influence of the Asn residue, with its -CH2-C(= O)-NH2 side chain, on the local conformational preferences of a peptide backbone. The double-resonance methods of resonant ion-dip infrared (RIDIR) spectroscopy and infrared-ultraviolet hole burning (IR-UV HB) spectroscopy were used to record single conformation spectra in the infrared and ultraviolet, respectively, free from interference from other conformations present in the molecular beam. Ac-Asn-NHBn spreads its population over two conformations, both of which bonds that form a bridge between the Asn carboxamide group and the NH and C = O groups on the peptide backbone. In one the peptide backbone engages in a 7-membered H-bonded ring (labeled C-eq(7)), thereby forming an inverse gamma-turn, stabilized by a C6/C7 Asn bridge. In the other the Asn carboxamide group forms a C8/C7 H-bonded bridge with the carboxamide group facing in the opposite direction across an extended peptide backbone involving a CS interaction. Both Ac-Ala-Asn-NHBn and Ac-Asn-Asn-NHBn are found exclusively in a single conformation in which the peptide backbone engages in a type I beta-turn with its C10 H-bond. The Asn residue(s) stabilize this beta-turn via C6 H-bond(s) between the carboxamide C = O group and the same residue's amide NH. These structures are closely analogous to the corresponding structures in Gin-containing peptides studied previously [Walsh, P. S. et al. PCCP 2016, 18, 11306-11322; Walsh, P. S. et al. Angew. Chem. Int. Ed. 2016, 55, 14618-14622], indicating that the Asn and Gln side chains can each configure so as to stabilize the same backbone conformations. Spectroscopic and computational evidence suggest that glutamine is more predisposed than asparagine to beta-turn formation via unusually strong s
机译：的串联封端的含天冬酰胺的肽，AC-ASN-NHBn，AC-ALA-ASN-NHBn，和Ac-ASN-ASN-NHBn，所述的红外线和紫外线光谱，在气相中被记录射流冷却的条件下为了探测Asn残基的影响，其-CH 2 -C（= O）-NH 2侧链上的肽主链的构象本地偏好。红外谐振离子浸的双谐振的方法（RIDIR）光谱法和红外紫外线烧孔（IR-UV HB）光谱被用于从其他构象本干扰分别记录在红外线和紫外线，单一构象光谱，自由在分子束。 AC-ASN-NHBn敷于其人口超过两种构象，这两者形成所述天冬酰胺酰胺基团和NH和C =对肽骨架Ô基之间的桥键的。在一个在一个7元H-结合的环肽骨架接合（标记为C-当量（7）），从而形成逆伽马转，由C6 / C7的Asn桥稳定。中的另一个中的Asn羧酰胺基团形成具有跨越涉及CS相互作用延长肽主链的相反方向面向所述羧酰胺基团的C8 / C7 H-粘结桥。两个AC-ALA-ASN-NHBn和Ac-ASN-ASN-NHBn在单一构象仅仅存在，其中，在I型β-转角与其C10 H-键的肽骨架接合。所述Asn残基（一个或多个）稳定经由C6 H-键（一个或多个）的甲酰胺C = O基团，并且在同一残基的酰胺NH之间的这种β-转角。这些结构是密切类似于相应结构在先前研究[沃尔什，P.S。等人含杜松子酒肽。 PCCP 2016，18，11306-11322;沃尔什，P.S。等人。 angew。化学。 int。编辑。 2016年，55，14618-14622]，表明Asn和谷氨酰胺的侧链可以各自配置，以便稳定相同的主链构象。光谱和计算的证据表明，谷氨酰胺多天冬酰胺的β-折叠通过形成异常强大的小号倾向

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