标题
Development and use of an atomistic CHARMM-based forcefield for peptoid simulation
作者
关键词
-
出版物
JOURNAL OF COMPUTATIONAL CHEMISTRY
Volume 35, Issue 5, Pages 360-370
出版商
Wiley
发表日期
2013-11-29
DOI
10.1002/jcc.23478
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone ϕ, ψ and Side-Chain χ1 and χ2 Dihedral Angles
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- Design and conformational analysis of peptoids containing N-hydroxy amides reveals a unique sheet-like secondary structure
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- Folding of a single-chain, information-rich polypeptoid sequence into a highly ordered nanosheet
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- Expanded Polyglutamine-Binding Peptoid as a Novel Therapeutic Agent for Treatment of Huntington's Disease
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- CHARMM Additive All-Atom Force Field for Carbohydrate Derivatives and Its Utility in Polysaccharide and Carbohydrate–Protein Modeling
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- Shaken, Not Stirred: Collapsing a Peptoid Monolayer To Produce Free-Floating, Stable Nanosheets
- (2011) Babak Sanii et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Engineered Biomimetic Polymers as Tunable Agents for Controlling CaCO3Mineralization
- (2011) Chun-Long Chen et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Long-Range Intra-Protein Communication Can Be Transmitted by Correlated Side-Chain Fluctuations Alone
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- Free-floating ultrathin two-dimensional crystals from sequence-specific peptoid polymers
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- A Preliminary Survey of the Peptoid Folding Landscape
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- Folded biomimetic oligomers for enantioselective catalysis
- (2009) G. Maayan et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Is Alanine Dipeptide a Good Model for Representing the Torsional Preferences of Protein Backbones?
- (2008) Michael Feig Journal of Chemical Theory and Computation
- Biomimetic Nanostructures: Creating a High-Affinity Zinc-Binding Site in a Folded Nonbiological Polymer
- (2008) Byoung-Chul Lee et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides
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