Comparative protein structure modeling of genes and genomes

MA Martí-Renom, AC Stuart, A Fiser… - Annual review of …, 2000 - annualreviews.org
▪ Abstract Comparative modeling predicts the three-dimensional structure of a given protein
sequence (target) based primarily on its alignment to one or more proteins of known …

Validation of protein crystal structures

GJ Kleywegt - Acta Crystallographica Section D: Biological …, 2000 - journals.iucr.org
Since the process of building and refining a model of a biomacromolecule based on
crystallographic data is subjective, quality-control techniques are required to assess the …

A series of PDB-related databanks for everyday needs

WG Touw, C Baakman, J Black… - Nucleic acids …, 2015 - academic.oup.com
We present a series of databanks (http://swift. cmbi. ru. nl/gv/facilities/) that hold information
that is computationally derived from Protein Data Bank (PDB) entries and that might …

The protein data bank

HM Berman, J Westbrook, Z Feng… - Nucleic acids …, 2000 - academic.oup.com
Abstract The Protein Data Bank (PDB; http://www. rcsb. org/pdb/) is the single worldwide
archive of structural data of biological macromolecules. This paper describes the goals of …

A series of PDB related databases for everyday needs

RP Joosten, TAH Te Beek, E Krieger… - Nucleic acids …, 2010 - academic.oup.com
Abstract The Protein Data Bank (PDB) is the world-wide repository of macromolecular
structure information. We present a series of databases that run parallel to the PDB. Each …

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

E Krieger, G Koraimann… - … : Structure, Function, and …, 2002 - Wiley Online Library
One of the conclusions drawn at the CASP4 meeting in Asilomar was that applying various
force fields during refinement of template‐based models tends to move predictions in the …

Making optimal use of empirical energy functions: force‐field parameterization in crystal space

E Krieger, T Darden, SB Nabuurs… - Proteins: Structure …, 2004 - Wiley Online Library
Today's energy functions are not able yet to distinguish reliably between correct and almost
correct protein models. Improving these near‐native models is currently a major bottle‐neck …

Objectively judging the quality of a protein structure from a Ramachandran plot

RWW Hooft, C Sander, G Vriend - Bioinformatics, 1997 - academic.oup.com
Motivation Statistical methods that compare observed and expected distributions of
experimental observables provide powerful tools for the quality control of protein structures …

[HTML][HTML] Prediction and reduction of the aggregation of monoclonal antibodies

R van der Kant, AR Karow-Zwick, J Van Durme… - Journal of molecular …, 2017 - Elsevier
Protein aggregation remains a major area of focus in the production of monoclonal
antibodies. Improving the intrinsic properties of antibodies can improve manufacturability …

Homology modeling, model and software evaluation: three related resources.

R Rodriguez, G Chinea, N Lopez… - Bioinformatics (Oxford …, 1998 - academic.oup.com
MOTIVATION: Homology modeling is rapidly becoming the method of choice for obtaining
three-dimensional coordinates for proteins because genome projects produce sequences at …