• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利：CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法，用中文像聊天一样搜索，搜遍4000万医学文献。AI智能推荐，让科研检索更轻松。

立即免费搜索

文件翻译

保留排版，准确专业，支持PDF/Word/PPT等文件格式，支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述，25分钟生成高质量综述，智能提取关键信息，辅助科研写作。

立即免费体验

相似文献

1
A procedure for the automatic determination of hydrophobic cores in protein structures.一种自动确定蛋白质结构中疏水核心的方法。
Protein Sci. 1995 Jan;4(1):93-102. doi: 10.1002/pro.5560040112.
2
Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chain contacts secondary structure and accessibility.在具有相似折叠结构的蛋白质中，结构特征可能是不保守的。对侧链与侧链接触、二级结构和可及性进行分析。
J Mol Biol. 1994 Dec 2;244(3):332-50. doi: 10.1006/jmbi.1994.1733.
3
An integrated approach to the analysis and modeling of protein sequences and structures. III. A comparative study of sequence conservation in protein structural families using multiple structural alignments.一种蛋白质序列与结构分析及建模的综合方法。III. 使用多重结构比对对蛋白质结构家族中的序列保守性进行比较研究。
J Mol Biol. 2000 Aug 18;301(3):691-711. doi: 10.1006/jmbi.2000.3975.
4
Protein topology recognition from secondary structure sequences: application of the hidden Markov models to the alpha class proteins.从二级结构序列识别蛋白质拓扑结构：隐马尔可夫模型在α类蛋白质中的应用。
J Mol Biol. 1997 Mar 28;267(2):446-63. doi: 10.1006/jmbi.1996.0874.
5
Folding the main chain of small proteins with the genetic algorithm.使用遗传算法折叠小蛋白质的主链。
J Mol Biol. 1994 Feb 25;236(3):844-61. doi: 10.1006/jmbi.1994.1193.
6
Comparison of the physiologically equivalent proteins cytochrome c6 and plastocyanin on the basis of their electrostatic potentials. Tryptophan 63 in cytochrome c6 may be isofunctional with tyrosine 83 in plastocyanin.基于生理等效蛋白细胞色素c6和质体蓝素的静电势进行比较。细胞色素c6中的色氨酸63可能与质体蓝素中的酪氨酸83具有同功功能。
Biochemistry. 1997 Dec 23;36(51):16187-96. doi: 10.1021/bi971241v.
7
Protein structure comparison by alignment of distance matrices.通过距离矩阵比对进行蛋白质结构比较。
J Mol Biol. 1993 Sep 5;233(1):123-38. doi: 10.1006/jmbi.1993.1489.
8
Differential stabilization of two hydrophobic cores in the transition state of the villin 14T folding reaction.在绒毛蛋白14T折叠反应过渡态中两个疏水核心的差异稳定性
J Mol Biol. 2000 Nov 17;304(1):99-115. doi: 10.1006/jmbi.2000.4190.
9
Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins.主链静电、疏水效应和侧链构象熵在决定蛋白质二级结构中的作用。
J Mol Biol. 1998 Jun 12;279(3):665-84. doi: 10.1006/jmbi.1998.1792.
10
De novo design of the hydrophobic cores of proteins.蛋白质疏水核心的从头设计。
Protein Sci. 1995 Oct;4(10):2006-18. doi: 10.1002/pro.5560041006.

引用本文的文献

1
StoneHinge: hinge prediction by network analysis of individual protein structures.StoneHinge：通过对单个蛋白质结构进行网络分析来预测铰链区
Protein Sci. 2009 Feb;18(2):359-71. doi: 10.1002/pro.38.
2
Probing protein mechanics: residue-level properties and their use in defining domains.探索蛋白质力学：残基水平特性及其在结构域定义中的应用
Biophys J. 2004 Sep;87(3):1426-35. doi: 10.1529/biophysj.104.042085.
3
Identification of compact, hydrophobically stabilized domains and modules containing multiple peptide chains.鉴定包含多条肽链的紧密、疏水稳定结构域和模块。
Protein Sci. 1997 Jun;6(6):1210-9. doi: 10.1002/pro.5560060609.
4
A procedure for the prediction of temperature-sensitive mutants of a globular protein based solely on the amino acid sequence.一种仅基于氨基酸序列预测球状蛋白温度敏感突变体的方法。
Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13908-13. doi: 10.1073/pnas.93.24.13908.
5
The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution.来自人类病原体克氏锥虫的锥虫硫醇还原酶在2.3埃分辨率下的晶体结构。
Protein Sci. 1996 Jan;5(1):52-61. doi: 10.1002/pro.5560050107.
6
A procedure for detecting structural domains in proteins.一种检测蛋白质中结构域的方法。
Protein Sci. 1995 Jan;4(1):103-12. doi: 10.1002/pro.5560040113.
7
Automatic recognition of hydrophobic clusters and their correlation with protein folding units.疏水簇的自动识别及其与蛋白质折叠单元的相关性。
Protein Sci. 1995 Jun;4(6):1188-202. doi: 10.1002/pro.5560040617.

本文引用的文献

1
Identification and classification of protein fold families.蛋白质折叠家族的识别与分类。
Protein Eng. 1993 Jul;6(5):485-500. doi: 10.1093/protein/6.5.485.
2
Protein structure comparison by alignment of distance matrices.通过距离矩阵比对进行蛋白质结构比较。
J Mol Biol. 1993 Sep 5;233(1):123-38. doi: 10.1006/jmbi.1993.1489.
3
A procedure for detecting structural domains in proteins.一种检测蛋白质中结构域的方法。
Protein Sci. 1995 Jan;4(1):103-12. doi: 10.1002/pro.5560040113.
4
How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins.不同的氨基酸序列如何决定相似的蛋白质结构：珠蛋白的结构与进化动力学
J Mol Biol. 1980 Jan 25;136(3):225-70. doi: 10.1016/0022-2836(80)90373-3.
5
Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin.中子衍射揭示了氧合肌红蛋白中的氧-组氨酸氢键。
Nature. 1981 Jul 2;292(5818):81-2. doi: 10.1038/292081a0.
6
Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains.由β-折叠形成的蛋白质的进化。II. 免疫球蛋白结构域的核心
J Mol Biol. 1982 Sep 15;160(2):325-42. doi: 10.1016/0022-2836(82)90179-6.
7
Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics.通过重新确定细胞色素b562的一级结构并使用分子图形技术改进其2.5埃分辨率模型。
J Mol Biol. 1981 Jun 5;148(4):427-48. doi: 10.1016/0022-2836(81)90185-6.
8
Evolution of proteins formed by beta-sheets. I. Plastocyanin and azurin.由β-折叠形成的蛋白质的进化。I. 质体蓝素和天青蛋白。
J Mol Biol. 1982 Sep 15;160(2):309-23. doi: 10.1016/0022-2836(82)90178-4.
9
The crystal structure of human deoxyhaemoglobin at 1.74 A resolution.分辨率为1.74埃的人脱氧血红蛋白晶体结构。
J Mol Biol. 1984 May 15;175(2):159-74. doi: 10.1016/0022-2836(84)90472-8.
10
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.蛋白质二级结构词典：氢键和几何特征的模式识别
Biopolymers. 1983 Dec;22(12):2577-637. doi: 10.1002/bip.360221211.

一种自动确定蛋白质结构中疏水核心的方法。

A procedure for the automatic determination of hydrophobic cores in protein structures.

作者信息

Swindells M B

机构信息

Protein Engineering Research Institute, Osaka, Japan.

出版信息

Protein Sci. 1995 Jan;4(1):93-102. doi: 10.1002/pro.5560040112.

DOI:10.1002/pro.5560040112
PMID:7773181
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2142969/
Abstract

An algorithm is described for automatically detecting hydrophobic cores in proteins of known structure. Three pieces of information are considered in order to achieve this goal. These are: secondary structure, side-chain accessibility, and side-chain-side-chain contacts. Residues are considered to contribute to a core when they occur in regular secondary structure and have buried side chains that form predominantly nonpolar contacts with one another. This paper describes the algorithm's application to families of proteins with conserved topologies but low sequence similarities. The aim of this investigation is to determine the efficacy of the algorithm as well as to study the extent to which similar cores are identified within a common topology.

摘要

本文描述了一种用于自动检测已知结构蛋白质中疏水核心的算法。为实现这一目标，考虑了三条信息。它们是：二级结构、侧链可及性和侧链-侧链接触。当残基出现在规则的二级结构中且具有埋藏的侧链，这些侧链彼此之间主要形成非极性接触时，就认为这些残基对核心有贡献。本文描述了该算法在具有保守拓扑结构但序列相似性较低的蛋白质家族中的应用。这项研究的目的是确定该算法的有效性，以及研究在共同拓扑结构中识别相似核心的程度。