(Q41938065)

English

The dominant role of side-chain backbone interactions in structural realization of amino acid code. ChiRotor: a side-chain prediction algorithm based on side-chain backbone interactions

scientific article published on 22 January 2007

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scholarly article

1 reference

Europe PubMed Central

14 October 2017

The dominant role of side-chain backbone interactions in structural realization of amino acid code. ChiRotor: a side-chain prediction algorithm based on side-chain backbone interactions (English)

1 reference

Europe PubMed Central

14 October 2017

3

0 references

author name string

Velin Z Spassov

1

1 reference

Europe PubMed Central

14 October 2017

Lisa Yan

2

1 reference

Europe PubMed Central

14 October 2017

Paul K Flook

3

1 reference

Europe PubMed Central

14 October 2017

publication date

22 January 2007

1 reference

Europe PubMed Central

14 October 2017

Protein Science

1 reference

Europe PubMed Central

14 October 2017

16

1 reference

Europe PubMed Central

14 October 2017

3

1 reference

Europe PubMed Central

14 October 2017

494-506

1 reference

Europe PubMed Central

14 October 2017

The dead-end elimination theorem and its use in protein side-chain positioning

1 reference

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Orientational potentials extracted from protein structures improve native fold recognition

1 reference

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Improved side-chain prediction accuracy using an ab initio potential energy function and a very large rotamer library

1 reference

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A graph-theory algorithm for rapid protein side-chain prediction

1 reference

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PISCES: a protein sequence culling server

1 reference

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GEM: a Gaussian Evolutionary Method for predicting protein side-chain conformations

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

5 June 2018

Side-chain modeling with an optimized scoring function

1 reference

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5 June 2018

Extending the accuracy limits of prediction for side-chain conformations

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

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Free energy determinants of tertiary structure and the evaluation of protein models.

1 reference

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Generalized born models of macromolecular solvation effects

1 reference

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Charge-charge interactions influence the denatured state ensemble and contribute to protein stability

1 reference

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Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect

1 reference

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Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability

1 reference

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Simplified methods for pKa and acid pH-dependent stability estimation in proteins: removing dielectric and counterion boundaries.

1 reference

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Optimization of the electrostatic interactions between ionized groups and peptide dipoles in proteins

1 reference

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All in one: a highly detailed rotamer library improves both accuracy and speed in the modelling of sidechains by dead-end elimination

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

5 June 2018

Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation correct?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

5 June 2018

Backbone-dependent rotamer library for proteins. Application to side-chain prediction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

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Optimization of the electrostatic interactions in proteins of different functional and folding type

1 reference

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Determinants of protein side-chain packing

1 reference

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The interpretation of protein structures: Estimation of static accessibility

1 reference

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Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes

1 reference

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Evaluation of protein models by atomic solvation preference.

1 reference

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Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins

1 reference

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Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

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Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: implications for protein design and structural genomics.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2203320

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Spatial optimization of electrostatic interactions between the ionized groups in globular proteins.

1 reference

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A method to configure protein side-chains from the main-chain trace in homology modelling

1 reference

https://pubmed.ncbi.nlm.nih.gov/17242380

12 December 2020

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Identifiers

10.1110/PS.062447107

1 reference

Europe PubMed Central

14 October 2017

1 reference

Europe PubMed Central

14 October 2017

1 reference

Europe PubMed Central

14 October 2017

ResearchGate publication ID

0 references

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