Structure by design: from single proteins and their building blocks to nanostructures.

Structure by design: from single proteins and their building blocks to nanostructures. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Structure by design: from single proteins and their building blocks to nanostructures. Abstract Text:

Chung-Jung Tsai,Jie Zheng,Carlos ,Ruth Nussinov,

Nanotechnology realizes the advantages of naturally occurring biological macromolecules and their building-block nature for design. Frequently, assembly starts with the choice of a "good" molecule that is synthetically optimized towards the desired shape. By contrast, we propose starting with a pre-specified nanostructure shape, selecting candidate protein building blocks from a library and mapping them onto the shape and, finally, testing the stability of the construct. Such a shape-based, part-assembly strategy is conceptually similar to protein design through the combinatorial assembly of building blocks. If the conformational preferences of the building blocks are retained and their interactions are favorable, the nanostructure will be stable. The richness of the conformations, shapes and chemistries of the protein building blocks suggests a broad range of potential applications; at the same time, it also highlights their complexity. In this Opinion article, we focus on the first step: validating such a strategy against experimental data.

Structure by design: from single proteins and their building blocks to nanostructures. Publishing Authors By Initials

CJ Tsai,J Zheng,C ,R Nussinov,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Structure by design: from single proteins and their building blocks to nanostructures. Journal Published:

PUBLICATION TYPE: Review

Journal: Trends in biotechnology

VOLUME: 24

Page Numbers: 449-54

Journal Abbreviation:

ISSN: 0167-7799

DAY: 28

MONTH: 08

YEAR: 2006

Structure by design: from single proteins and their building blocks to nanostructures. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8310903

Structure by design: from single proteins and their building blocks to nanostructures. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Structure by design: from single proteins and their building blocks to nanostructures. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Structure by design: from single proteins and their building blocks to nanostructures.

AFFILIATION: Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA.

Country: England

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Trends Biotechnol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Structure by design: from single proteins and their building blocks to nanostructures Related Publications

• "Similarity trap" in protein-protein interactions could be carcinogenic: simulations of p53 core domain complexed with 53BP1 and BRCA1 BRCT domains.
• A hierarchical protein folding scheme based on the building block folding model.
• Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design.
• Allostery: Absence of a Change in Shape Does Not Imply that Allostery Is Not at Play.
• Backbone conformational preferences and pseudorotational ring puckering of 1-aminocyclopentane-1-carboxylic acid.
• Changing the charge distribution of beta-helical-based nanostructures can provide the conditions for charge transfer.
• Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect.
• Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure.
• Designing a nanotube using naturally occurring protein building blocks.
• How different are structurally flexible and rigid binding sites? Sequence and structural features discriminating proteins that do and do not undergo conformational change upon ligand binding.
• Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.
• Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities.
• Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process.
• Modular architecture of protein structures and allosteric communications: potential implications for signaling proteins and regulatory linkages.
• MolAxis: a server for identification of channels in macromolecules.
• Molecular dynamics simulations of Alzheimer Abeta40 elongation and lateral association.
• Nanostructure design using protein building blocks enhanced by conformationally constrained synthetic residues.
• New structures help the modeling of toxic amyloidss ion channels.
• Principles of nanostructure design with protein building blocks.
• Residue centrality, functionally important residues, and active site shape: analysis of enzyme and non-enzyme families.
• Sequence analysis of p53 response-elements suggests multiple binding modes of the p53 tetramer to DNA targets.
• Similar binding sites and different partners: implications to shared proteins in cellular pathways.
• Simulations as analytical tools to understand protein aggregation and predict amyloid conformation.
• Structural basis for p53 binding-induced DNA bending.
• Structural dynamics of the cooperative binding of organic molecules in the human cytochrome P450 3A4.
• Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35.
• Structure by design: from single proteins and their building blocks to nanostructures.
• Towards drugs targeting multiple proteins in a systems biology approach.
• Trp/Met/Phe hot spots in protein-protein interactions: potential targets in drug design.
• p53-Induced DNA bending: the interplay between p53-DNA and p53-p53 interactions.