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来自古细菌巴氏甲烷八叠球菌的染色体蛋白HMb的一级结构。

Primary structure of the chromosomal protein HMb from the archaebacteria Methanosarcina barkeri.

作者信息

Laine B, Chartier F, Imbert M, Lewis R, Sautiere P

出版信息

Eur J Biochem. 1986 Dec 15;161(3):681-7. doi: 10.1111/j.1432-1033.1986.tb10493.x.

Abstract

The amino acid sequence of the protein HMb, a protein of 93 residues (Mr 10757) which represents the major acid-soluble component of the Methanosarcina barkeri nucleoprotein complex, has been established from automated sequence analysis of the protein and from structural data provided by peptides derived from cleavage of the protein at aspartic acid, arginine and methionine residues. The protein HMb is mainly characterized by a high amount of charged residues (15% of acidic residues and 26.8% of basic residues) which are distributed all along the polypeptide chain. The amino acid sequence of the protein HMb is not homologous to any eubacterial, archaebacterial or eukaryotic chromosomal proteins known up to now.

摘要

蛋白质HMb由93个氨基酸残基组成(分子量为10757),是巴氏甲烷八叠球菌核蛋白复合体中主要的酸溶性成分。通过对该蛋白质的自动序列分析以及对该蛋白质在天冬氨酸、精氨酸和甲硫氨酸残基处裂解产生的肽段所提供的结构数据,已确定了其氨基酸序列。蛋白质HMb的主要特征是沿着多肽链分布着大量带电荷的残基(酸性残基占15%,碱性残基占26.8%)。到目前为止,蛋白质HMb的氨基酸序列与任何已知的真细菌、古细菌或真核染色体蛋白质都不同源。

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