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短杆菌肽K的分子和通道形成特性:一类天然存在的酰化短杆菌肽。

Molecular and channel-forming characteristics of gramicidin K's: a family of naturally occurring acylated gramicidins.

作者信息

Williams L P, Narcessian E J, Andersen O S, Waller G R, Taylor M J, Lazenby J P, Hinton J F, Koeppe R E

机构信息

Department of Physiology and Biophysics, Cornell University Medical College, New York, New York 10021.

出版信息

Biochemistry. 1992 Aug 18;31(32):7311-9. doi: 10.1021/bi00147a015.

DOI:10.1021/bi00147a015
PMID:1380823
Abstract

The gramicidin K family is a set of naturally occurring acylated linear peptides in which a fatty acid is esterified to the ethanolamine hydroxyl of either gramicidin A or C, and possibly also to gramicidin B (Koeppe, R. E., II, Paczkowski, J. A., & Whaley, W. L. (1985) Biochemistry 24, 2822-2826). These acylated gramicidins form membrane-spanning channels in planar lipid bilayers and therefore constitute a model system with which to study the structural and functional consequences of acylation on membrane proteins. This paper serves to characterize further the channels formed by acylated gramicidins A and C and to demonstrate that these channels are structurally equivalent to the channels formed by the standard gramicidins. We also present additional evidence for the ester linkage in the natural acylated gramicidins A and C and identify the fatty acyl chains.

摘要

短杆菌肽K家族是一组天然存在的酰化线性肽,其中脂肪酸被酯化到短杆菌肽A或C的乙醇胺羟基上,也可能酯化到短杆菌肽B上(科佩,R.E.二世,帕乔夫斯基,J.A.,& 惠利,W.L.(1985年)《生物化学》24卷,2822 - 2826页)。这些酰化短杆菌肽在平面脂质双分子层中形成跨膜通道,因此构成了一个用于研究酰化对膜蛋白结构和功能影响的模型系统。本文旨在进一步表征酰化短杆菌肽A和C形成的通道,并证明这些通道在结构上等同于标准短杆菌肽形成的通道。我们还提供了关于天然酰化短杆菌肽A和C中酯键的额外证据,并鉴定了脂肪酰链。

相似文献

1
Molecular and channel-forming characteristics of gramicidin K's: a family of naturally occurring acylated gramicidins.短杆菌肽K的分子和通道形成特性:一类天然存在的酰化短杆菌肽。
Biochemistry. 1992 Aug 18;31(32):7311-9. doi: 10.1021/bi00147a015.
2
Gramicidins A, B, and C form structurally equivalent ion channels.短杆菌肽A、B和C形成结构等效的离子通道。
Biophys J. 1990 Nov;58(5):1207-12. doi: 10.1016/S0006-3495(90)82461-9.
3
Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association.脂双层中短杆菌肽通道形成的动力学:跨膜单体缔合
Science. 1990 Nov 30;250(4985):1256-9. doi: 10.1126/science.1700867.
4
Synthesis of acylated gramicidins and the influence of acylation on the interfacial properties and conformational behavior of gramicidin A.酰化短杆菌肽的合成以及酰化对短杆菌肽A界面性质和构象行为的影响。
Biochim Biophys Acta. 1991 Nov 4;1069(2):157-64. doi: 10.1016/0005-2736(91)90118-r.
5
Influence of acylation on the channel characteristics of gramicidin A.酰化对短杆菌肽A通道特性的影响。
Biochemistry. 1992 Aug 18;31(32):7320-4. doi: 10.1021/bi00147a016.
6
Formation of non-beta 6.3-helical gramicidin channels between sequence-substituted gramicidin analogues.序列取代的短杆菌肽类似物之间形成非β 6.3螺旋短杆菌肽通道。
Biophys J. 1992 Apr;62(1):145-57; discussion 157-9. doi: 10.1016/S0006-3495(92)81801-5.
7
Energetics of gramicidin hybrid channel formation as a test for structural equivalence. Side-chain substitutions in the native sequence.作为结构等效性测试的短杆菌肽杂交通道形成的能量学。天然序列中的侧链取代。
J Mol Biol. 1990 Jan 5;211(1):221-34. doi: 10.1016/0022-2836(90)90022-E.
8
Asymmetric gramicidin channels: heterodimeric channels with a single F6Val1 residue.不对称短杆菌肽通道:具有单个F6Val1残基的异二聚体通道。
Biophys J. 1994 Jun;66(6):1823-32. doi: 10.1016/S0006-3495(94)80976-2.
9
Gramicidin channels--a solvable membrane "protein" folding problem.短杆菌肽通道——一个可解决的膜“蛋白”折叠问题。
Indian J Biochem Biophys. 1996 Oct;33(5):331-42.
10
Palmitoylation-induced conformational changes of specific side chains in the gramicidin transmembrane channel.短杆菌肽跨膜通道中棕榈酰化诱导的特定侧链构象变化。
Biochemistry. 1995 Jul 25;34(29):9299-306. doi: 10.1021/bi00029a004.

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Effects of phenylalanine substitutions in gramicidin A on the kinetics of channel formation in vesicles and channel structure in SDS micelles.短杆菌肽A中苯丙氨酸取代对囊泡中通道形成动力学及SDS胶束中通道结构的影响。
Biophys J. 2005 Jan;88(1):224-34. doi: 10.1529/biophysj.104.047456. Epub 2004 Oct 22.
2
Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy.基于氘核磁共振光谱法的短杆菌肽通道中色氨酸9和11侧链的取向
Biophys J. 1994 Jan;66(1):14-24. doi: 10.1016/S0006-3495(94)80748-9.