TSAR, a new graph-theoretical approach to computational modeling of protein side-chain flexibility: modeling of ionization properties of proteins. (Q51547005)

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scientific article published on 18 July 2011

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English	TSAR, a new graph-theoretical approach to computational modeling of protein side-chain flexibility: modeling of ionization properties of proteins.	scientific article published on 18 July 2011

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

TSAR, a new graph-theoretical approach to computational modeling of protein side-chain flexibility: modeling of ionization properties of proteins. (English)

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

computational biology

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based on heuristic

inferred from title

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based on heuristic

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author name string

Oleg V Stroganov

1

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

Fedor N Novikov

2

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

Alexey A Zeifman

3

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

Viktor S Stroylov

4

1 reference

Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

Ghermes G Chilov

5

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

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publication date

18 July 2011

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

79

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

9

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

2693-2710

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Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

Modeling electrostatic effects in proteins

1 reference

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Calculations of electrostatic interactions in biological systems and in solutions

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pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model

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A self-consistent, microenvironment modulated screened coulomb potential approximation to calculate pH-dependent electrostatic effects in proteins

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Complexity of Finding Embeddings in a k-Tree

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Enhanced dead-end elimination in the search for the global minimum energy conformation of a collection of protein side chains

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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.

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Macroscopic models for studies of electrostatic interactions in proteins: limitations and applicability

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Electrostatic effects in proteins: comparison of dielectric and charge models

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21 January 2018

What are the dielectric "constants" of proteins and how to validate electrostatic models?

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PPD v1.0--an integrated, web-accessible database of experimentally determined protein pKa values

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Individual ionization constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR.

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21 January 2018

Very fast empirical prediction and rationalization of protein pKa values

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21 January 2018

Optimizing the hydrogen-bond network in Poisson-Boltzmann equation-based pK(a) calculations.

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21 January 2018

Measurement of the individual pKa values of acidic residues of hen and turkey lysozymes by two-dimensional 1H NMR.

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Energy functions for protein design I: efficient and accurate continuum electrostatics and solvation

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Automated sampling assessment for molecular simulations using the effective sample size

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21 January 2018

Identifiers

10.1002/PROT.23099

1 reference

Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 April 2018

http://europepmc.org/abstract/MED/21769942

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