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本文引用的文献

1
Large Circular Dichroism Ellipticities for N-Templated Helical Polypeptides Are Inconsistent with Currently Accepted Helicity Algorithms.N-模板化螺旋多肽的大园二色性椭圆率与目前公认的螺旋度算法不一致。
Angew Chem Int Ed Engl. 1999 May 3;38(9):1290-1292. doi: 10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E.
2
Determination of H(N),H (α) and H (N),C' coupling constants in (13)C, (15)N-labeled proteins.测定（13）C、（15）N 标记蛋白质中的 H（N）、H（α）和 H（N）、C'耦合常数。
J Biomol NMR. 1994 Mar;4(2):231-40. doi: 10.1007/BF00175250.
3
DETERMINATION OF THE PARAMETERS FOR HELIX FORMATION IN POLY-gamma-BENZYL-L-GLUTAMATE.聚-γ-苄基-L-谷氨酸中螺旋形成参数的测定
Proc Natl Acad Sci U S A. 1959 Nov;45(11):1601-7. doi: 10.1073/pnas.45.11.1601.
4
The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.蛋白质的结构；多肽链的两种氢键螺旋构型。
Proc Natl Acad Sci U S A. 1951 Apr;37(4):205-11. doi: 10.1073/pnas.37.4.205.
5
H-bonding cooperativity and energetics of alpha-helix formation of five 17-amino acid peptides.五条17氨基酸肽的α-螺旋形成中的氢键协同性和能量学
J Am Chem Soc. 2003 Jul 9;125(27):8124-9. doi: 10.1021/ja035302q.
6
Dual wavelength parametric test of two-state models for circular dichroism spectra of helical polypeptides: anomalous dichroic properties of alanine-rich peptides.螺旋多肽圆二色光谱双态模型的双波长参数测试：富含丙氨酸肽的异常二色性特性
J Am Chem Soc. 2003 Feb 5;125(5):1203-20. doi: 10.1021/ja0275360.
7
Circular dichroism spectra of short, fixed-nucleus alanine helices.短的、固定核的丙氨酸螺旋的圆二色光谱。
Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15416-21. doi: 10.1073/pnas.232591399. Epub 2002 Nov 11.
8
Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques.富含谷氨酰胺和富含天冬酰胺结构域的Sup35中谷氨酰胺和丙氨酸重复序列扩展的蛋白质，以及淀粉样斑块中淀粉样β肽的聚集。
Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5596-600. doi: 10.1073/pnas.042681599.
9
Transforming growth factor beta receptor 1 polyalanine polymorphism and exon 5 mutation analysis in breast and ovarian cancer.
Cancer Epidemiol Biomarkers Prev. 2002 Feb;11(2):211-4.
10
Solubilized, spaced polyalanines: a context-free system for determining amino acid alpha-helix propensities.可溶解的、间隔排列的聚丙氨酸：一种用于确定氨基酸α-螺旋倾向的无背景系统。
J Am Chem Soc. 2002 Feb 13;124(6):945-62. doi: 10.1021/ja011726d.

水溶、帽稳定化的螺旋聚丙氨酸：用于核磁共振和圆二色性分析的校准标准品

Water-solubilized, cap-stabilized, helical polyalanines: calibration standards for NMR and CD analyses.

作者信息

Heitmann Björn, Job Gabriel E, Kennedy Robert J, Walker Sharon M, Kemp Daniel S

机构信息

Department of Chemistry, Room 18-296, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

出版信息

J Am Chem Soc. 2005 Feb 16;127(6):1690-704. doi: 10.1021/ja0457462.

DOI:10.1021/ja0457462
PMID:15701003
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1941670/
Abstract

NMR and CD studies are reported for two length series of solubilized, spaced, highly helical polyalanines that are N-capped by the optimal helix stabilizer (beta)Asp-Hel and C-capped by beta-aminoalanine beta and that are studied in water at 2 degrees C, pH 1-8. NMR analysis yields a structural characterization of the peptide Ac(beta)AspHelAla(8)betaNH(2) and selected members of one (beta)AspHelAla(n)beta series. At pH > 4.5 the (beta)AspHel cap provides a preorganized triad of carboxylate anion and two amide residues that is complementary to the helical polyalanine N-terminus. The C-terminal beta-aminoalanine assumes a helix-stabilizing conformation consistent with literature precedents. H(N)CO NMR experiments applied to capped, uniformly (13)C- and (15)N-labeled Ala(8) and Ala(12) peptides define Ala(n) hydrogen bonding signatures as alpha-helical without detectable 3(10) character. Relative NH-->ND exchange rates yield site protection factors PF(i) that define uniquely high fractional helicities FH for the peptide Ala(n) regions. These Ala(n) calibration series, studied in water and lacking helix-stabilizing tertiary structure, yield the first (13)C NMR chemical shifts, (3)J(HNH)(alpha) coupling constants, and CD ellipticities theta(Molar) characteristic of a fully helical alanine within an Ala(n) context. CD data are used to assign parameters X and theta, required for rigorous calculation of FH values from CD ellipticities.

摘要

本文报道了两个长度系列的可溶解、间隔排列、高度螺旋化的聚丙氨酸的核磁共振（NMR）和圆二色性（CD）研究。这些聚丙氨酸的N端由最佳螺旋稳定剂（β）天冬氨酸-螺旋（Asp-Hel）封端，C端由β-氨基丙氨酸封端，在2℃、pH值为1 - 8的水中进行研究。NMR分析给出了肽Ac（β）AspHelAla（8）βNH₂以及一个（β）AspHelAla（n）β系列中选定成员的结构特征。在pH > 4.5时，（β）AspHel封端提供了一个预先组织好的由羧酸根阴离子和两个酰胺残基组成的三联体，它与螺旋聚丙氨酸的N端互补。C端的β-氨基丙氨酸呈现出与文献先例一致的螺旋稳定构象。应用于封端的、均匀¹³C和¹⁵N标记的Ala（8）和Ala（12）肽的¹H¹³C NMR实验确定了Ala（n）的氢键特征为α-螺旋，没有可检测到的3¹⁰特征。相对的NH→ND交换率产生了位点保护因子PF（i），它唯一地定义了肽Ala（n）区域的高分数螺旋度FH。这些在水中研究且缺乏螺旋稳定三级结构的Ala（n）校准系列，给出了第一个¹³C NMR化学位移、³J（HNH）α耦合常数以及在Ala（n）环境中完全螺旋化丙氨酸的CD椭圆率[θ（摩尔）]（λ，n）。CD数据用于确定从CD椭圆率严格计算FH值所需的参数X和θ（λ，∞）。