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Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions.

作者信息

Kowalczykowski S C, Lonberg N, Newport J W, von Hippel P H

出版信息

J Mol Biol. 1981 Jan 5;145(1):75-104. doi: 10.1016/0022-2836(81)90335-1.

DOI:10.1016/0022-2836(81)90335-1
PMID:7265204
Abstract
摘要

相似文献

1
Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions.噬菌体T4编码的基因32蛋白与核酸的相互作用。I. 结合相互作用的特性
J Mol Biol. 1981 Jan 5;145(1):75-104. doi: 10.1016/0022-2836(81)90335-1.
2
Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32P*III).
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Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA.噬菌体T4编码的基因32蛋白与核酸的相互作用。II. 与DNA和RNA结合的特异性
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Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (helix destabilizing) protein with single-stranded nucleic acids. Evidence for protein translocation.噬菌体T4基因32（解螺旋）蛋白与单链核酸结合的动力学及机制。蛋白转位的证据。
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A maximum of two tryptophan residues in gene-32 protein from phage T4 undergo stacking interactions with single-stranded polynucleotides.来自噬菌体T4的基因32蛋白中最多有两个色氨酸残基与单链多核苷酸发生堆积相互作用。
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On the thermodynamics and kinetics of the cooperative binding of bacteriophage T4-coded gene 32 (helix destabilizing) protein to nucleic acid lattices.关于噬菌体T4编码的基因32（解螺旋）蛋白与核酸晶格协同结合的热力学和动力学
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