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Open AccessJournal ArticleDOI

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

Rob Hooft, +2 more
- 01 Aug 1997 - 
- Vol. 13, Iss: 4, pp 425-430
TLDR
A new and-simple method is presented for judging the quality of a protein structure based on the distribution of backbone dihedral angles, resulting in a Ramachandran Z-score, expressing thequality of the Ramach andran plot relative to current state-of-the-art structures.
Abstract
Motivation: Statistical methods that compare observed and expected distributions of experimental observables provide powerful tools for the quality control of protein structures. The distribution of backbone dihedral angles ('Ramachandran plot') has often been used for such quality control, but without a firm statistical foundation. Results: A new and simple method is presented for judging the quality of a protein structure based on the distribution of backbone dihedral angles. Inputs to the method are 60 torsion angle distributions extracted from protein structures solved at high resolution; one for each combination of residue type and tri-state secondary structure. Output for a protein is a Ramachandran Z-score, expressing the quality of the Ramachandran plot relative to current state-of-the-art structures.

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TL;DR: Algorithms are presented that allowed a web-server implementation of PDB_REDO, and the first user results are discussed.
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Refinement of protein structures in explicit solvent.

TL;DR: The results demonstrate the significant improvement of structure quality by a short refinement in a thin layer of solvent and show that a dihedral angle energy term in the force field is beneficial for structure calculation and refinement.
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The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions.

TL;DR: Investigation of the influence of electrostatic surface potential distribution of monoclonal antibodies (MAbs) on intermolecular interactions and viscosity finds replacement of charge residues in the sequence of MAb-2, M-10, did not invoke charge distribution to the same extent as M Ab-1 and hence exhibited a similar viscolysis and self-association profile as Mab-2.
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The interrelationships of side-chain and main-chain conformations in proteins.

TL;DR: Analyses of residues occurring with disallowed main-chain conformation or with multiple conformations shed some light on why some residues are less favoured in thermophiles.
References
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Journal ArticleDOI

PROCHECK: a program to check the stereochemical quality of protein structures

TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
Journal ArticleDOI

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

TL;DR: A set of simple and physically motivated criteria for secondary structure, programmed as a pattern‐recognition process of hydrogen‐bonded and geometrical features extracted from x‐ray coordinates is developed.
Journal ArticleDOI

The Protein Data Bank: a computer-based archival file for macromolecular structures.

TL;DR: The Protein Data Bank is a computer-based archival file for macromolecular structures that stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies.
Journal ArticleDOI

WHAT IF: A molecular modeling and drug design program

TL;DR: The menu-driven operation of WHAT IF, combined with the use of default values wherever user input is required, makes it very easy to use for a novice user while keeping full flexibility for more sophisticated studies.
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