磷脂囊泡中短杆菌肽A通道的构象：一项碳-13和氟-19核磁共振研究。
Conformation of gramicidin A channel in phospholipid vesicles: a 13C and 19F nuclear magnetic resonance study.
作者信息
Weinstein S, Wallace B A, Blout E R, Morrow J S, Veatch W
出版信息
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4230-4. doi: 10.1073/pnas.76.9.4230.
Abstract
We have determined the conformation of the channel-forming polypeptide antibiotic gramicidin A in phosphatidylcholine vesicles by using 13C and 19F NMR spectroscopy. The models previously proposed for the conformation of the dimer channel differ in the surface localization of the NH2 and COOH termini. We have incorporated specific 13C and 19F nuclei at both the NH2, and COOH termini of gramicidin and have used 13C and 19F chemical shifts and spin lattice relaxation time measurements to determine the accessibility of these labels to three paramagnetic NMR probes--two in aqueous solution and one attached to the phosphatidylcholine fatty acid chain9 all of our results indicate that the COOH terminus of gramicidin in the channel is located near the surface of the membrane and the NH2 terminus is buried deep within the lipid bilayer. These findings strongly favor an NH2-terminal to NH2-terminal helical dimer as the major conformation for the gramicidin channel in phosphatidylcholine vesicles.
摘要
我们通过使用碳-13和氟-19核磁共振光谱法，确定了通道形成型多肽抗生素短杆菌肽A在磷脂酰胆碱囊泡中的构象。先前提出的二聚体通道构象模型在氨基和羧基末端的表面定位上存在差异。我们在短杆菌肽的氨基和羧基末端都引入了特定的碳-13和氟-19原子核，并利用碳-13和氟-19化学位移以及自旋晶格弛豫时间测量，来确定这些标记物对三种顺磁核磁共振探针的可及性——两种在水溶液中，一种连接在磷脂酰胆碱脂肪酸链上。我们所有的结果表明，通道中短杆菌肽的羧基末端位于膜表面附近，而氨基末端深埋在脂质双层内。这些发现强烈支持以氨基末端到氨基末端的螺旋二聚体作为磷脂酰胆碱囊泡中短杆菌肽通道的主要构象。
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Conformation of gramicidin A channel in phospholipid vesicles: a 13C and 19F nuclear magnetic resonance study.磷脂囊泡中短杆菌肽A通道的构象：一项碳-13和氟-19核磁共振研究。
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4230-4. doi: 10.1073/pnas.76.9.4230.
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