Peptide crystal growth via vapor diffusion. Crystal structure of glycyl-L-tyrosyl-L-alanine dihydrate.

D S Eggleston, P W Baures
{"title":"Peptide crystal growth via vapor diffusion. Crystal structure of glycyl-L-tyrosyl-L-alanine dihydrate.","authors":"D S Eggleston,&nbsp;P W Baures","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The structure of a dihydrated form of glycyl-L-tyrosyl-L-alanine (GYA) has been determined as part of a series of peptide structural investigations and development of microscale vapor diffusion experiments for peptide crystal growth. Crystals were grown by the hanging-drop method against sodium acetate. The tripeptide is a zwitterion in the crystal, adopting an extended conformation through glycine, a nearly perpendicular bend at tyrosine and a reverse turn for the C-terminal carboxylate. Principal backbone torsion angles are psi 1 175(1) degrees, omega 2 173(1) degrees, phi 2 -119(1) degrees, psi 2 120(1) degrees, omega 3 172(1) degrees, phi 3 -73(1) degrees, psi 31 -9(1) degrees, psi 32 171(1) degrees. The tyrosyl side chain adopts an unusual orientation (chi 1/2 = -86(1) degrees). The relationship of the GYA.2H2O structure to GYA sequences in proteins is examined, particularly as regards its helix-forming potential. Crystal data: C14H19N3O4.2H2O, M(r) = 345.36, orthorhombic, P2(1)2(1)2(1), a = 4.810 (4), b = 11.400(7), c = 30.162(23)A, V = 1653.8(24)A-3, Z = 4, Dx = 1.387 Mgm-3, lambda(CuK- alpha) = 1.540 A, mu = 9.053 mm-1, F(000) = 736, T = 199 K, R = 0.041 for 1458 observations with I greater than or equal to 3 sigma(I).</p>","PeriodicalId":14204,"journal":{"name":"International journal of peptide and protein research","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1992-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International journal of peptide and protein research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

The structure of a dihydrated form of glycyl-L-tyrosyl-L-alanine (GYA) has been determined as part of a series of peptide structural investigations and development of microscale vapor diffusion experiments for peptide crystal growth. Crystals were grown by the hanging-drop method against sodium acetate. The tripeptide is a zwitterion in the crystal, adopting an extended conformation through glycine, a nearly perpendicular bend at tyrosine and a reverse turn for the C-terminal carboxylate. Principal backbone torsion angles are psi 1 175(1) degrees, omega 2 173(1) degrees, phi 2 -119(1) degrees, psi 2 120(1) degrees, omega 3 172(1) degrees, phi 3 -73(1) degrees, psi 31 -9(1) degrees, psi 32 171(1) degrees. The tyrosyl side chain adopts an unusual orientation (chi 1/2 = -86(1) degrees). The relationship of the GYA.2H2O structure to GYA sequences in proteins is examined, particularly as regards its helix-forming potential. Crystal data: C14H19N3O4.2H2O, M(r) = 345.36, orthorhombic, P2(1)2(1)2(1), a = 4.810 (4), b = 11.400(7), c = 30.162(23)A, V = 1653.8(24)A-3, Z = 4, Dx = 1.387 Mgm-3, lambda(CuK- alpha) = 1.540 A, mu = 9.053 mm-1, F(000) = 736, T = 199 K, R = 0.041 for 1458 observations with I greater than or equal to 3 sigma(I).

分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
通过蒸汽扩散生长肽晶体。二水合甘酰基-酪氨酸-丙氨酸的晶体结构。
二水合形式的甘酰基- l-酪氨酸- l-丙氨酸(GYA)的结构已经确定,作为肽结构研究和微尺度蒸汽扩散实验的一部分,用于肽晶体生长。用悬滴法在乙酸钠环境下生长晶体。该三肽在晶体中为两性离子,在甘氨酸处呈延伸构象,在酪氨酸处呈几乎垂直的弯曲,在c端羧酸盐处呈相反的弯曲。主要的骨干扭力角是psi 1 175(1)度,omega 2 173(1)度,phi 2 -119(1)度,psi 2 120(1)度,omega 3 172(1)度,psi 3 -73(1)度,psi 31 -9(1)度,psi 32 171(1)度。酪氨酸侧链的取向不同寻常(chi 1/2 = -86(1)度)。研究了GYA. 2h2o结构与蛋白质中GYA序列的关系,特别是关于其螺旋形成潜力。晶体数据:C14H19N3O4.2H2O, M(r) = 345.36,正交,P2(1)2(1)2(1), a = 4.810 (4), b = 11.400(7), c = 30.162(23) a, V = 1653.8(24) a -3, Z = 4, Dx = 1.387 mg -3, lambda(CuK- alpha) = 1.540 a, mu = 9.053 mm-1, F(000) = 736, T = 199 K, r = 0.041, I大于等于3 sigma(I)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Noninvasive continuous monitoring of solid-phase peptide synthesis by acid-base indicator. Effect of aromatic amino acid substitutions in the 3-position of cyclic beta-casomorphin analogues on mu-opioid agonist/delta-opioid antagonist properties. Conformational investigation of alpha,beta-dehydropeptides. VII. Conformation of Ac-Pro-deltaAla-NHCH3 and Ac-Pro-(E)-deltaAbu-NHCH3: comparison with (Z)-substituted alpha,beta-dehydropeptides. Protease-catalyzed synthesis of Leu-enkephalin in a solvent-free system. beta-endorphin1-31 in the rat pituitary.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1