Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences.

Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences. Research Abstract Details 

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Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences. Abstract Text:

David Zanuy,Francisco ,Nurit Haspel,Jie Zheng,Ruth Nussinov,Carlos Aleman,David Zanuy,Francisco ,Nurit Haspel,Jie Zheng,Ruth Nussinov,Carlos Aleman,David Zanuy,Francisco ,Nurit Haspel,Jie Zheng,Ruth Nussinov,Carlos Aleman,

In this work we used atomistic molecular dynamics simulations to examine different aspects of tubular nanostructures constructed using protein building blocks with a beta-helical conformation. Initially, we considered two different natural protein building blocks, which were extracted from the protein data base, to compare the relative stabilities of the nanotubes obtained made of self-assembled and covalently linked repeats. Results show nanotubes constructed by linking building blocks through covalent bonds are very stable suggesting that the basic principles of polymer physics are valid when the repeating units are made of large fragments of proteins. In contrast, the stability of self-assembled nanostructures strongly depends on the attractive nonbonding interactions associated to building blocks aligned in a complementary manner. On the other hand, we investigated the ability of a conformationally constrained synthetic amino acid to enhance the stability of both self-assembled and polymerized nanotubes when it is used to substitute natural residues. Specifically, we considered 1-aminocyclopentane-1-caboxylic acid, which involves strong stereochemical constraints produced by the cyclopentane side chain. We found that the incorporation of this amino acid within the more flexible regions of the beta-helical building blocks is an excellent strategy to enhance the stability of the nanotubes. Thus, when a single mutation is performed in the loop region of the beta-helix, the bend architecture of the whole loop is stabilized since the conformational mobility is reduced not only at the mutated position but also at the adjacent positions.

Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences. Publishing Authors By Initials

D Zanuy,F ,N Haspel,J Zheng,R Nussinov,C Aleman,D Zanuy,F ,N Haspel,J Zheng,R Nussinov,C Aleman,D Zanuy,F ,N Haspel,J Zheng,R Nussinov,C Aleman,

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Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biomacromolecules

VOLUME: 8

Page Numbers: 3135-46

Journal Abbreviation: Biomacromolecules

ISSN: 1525-7797

DAY: 14

MONTH: 09

YEAR: 2007

Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences. Information

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LANGUAGE: eng

NlmUniqueID: 100892849

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Grant and Affiliation Information for Stability of tubular structures based on beta-helical proteins: self-assembled versus polymerized nanoconstructs and wild-type versus mutated sequences.

AFFILIATION: Departament d'Enginyeria Química, ETS d'Enginyeria Industrial de Barcelona, Universitat Politècnica de Catalunya, Diagonal 647, Barcelona, Spain. david.zanuy@upc.es

Country: United States

AGENCY: United States NCI

GRANT: N01 CO12400

ACRONYM: CO

MEDLINETA: Biomacromolecules

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