(Q28874041)

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Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field

scientific article (publication date: 15 May 2002)

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Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field (English)

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3

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Günther Koraimann

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Günther Koraimann

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2

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Elmar Krieger

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1

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English

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15 May 2002

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47

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393-402

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3

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The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

All-atom empirical potential for molecular modeling and dynamics studies of proteins

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Implicit solvent models

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Dynamical theory of activated processes in globular proteins

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Molecular simulation study of cooperativity in hydrophobic association

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Influence of rotational energy barriers to the conformational search of protein loops in molecular dynamics and ranking the conformations.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Energy refinement of hen egg-white lysozyme

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

SMILES, a chemical language and information system. 1. Introduction to methodology and encoding rules

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Improved simulation of liquid water by molecular dynamics

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Protein structure comparison by alignment of distance matrices

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

WHAT IF: a molecular modeling and drug design program

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

The 1.2 A crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged inhibitors

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.10104

retrieved

21 January 2018

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

(Q28874041)

Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field

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