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Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques. Structural alignment can therefore be used to imply evolutionary relationships between proteins that share very little common sequence. However, caution should be used in using the results as evidence for shared evolutionary ancestry because of the possible confounding effects of convergent evolution by which multiple unrelated amino acid sequences converge on a common tertiary structure.
Structural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds and local motifs, principles of molecular folding, evolution, binding interactions, and structure/function relationships, working both from experimentally solved structures and from computational models. The term structural has the same meaning as in structural biology, and structural bioinformatics can be seen as a part of computational structural biology. The main objective of structural bioinformatics is the creation of new methods of analysing and manipulating biological macromolecular data in order to solve problems in biology and generate new knowledge.
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In the context of chemistry, molecular physics and physical chemistry and molecular modelling, a force field is a computational model that is used to describe the forces between atoms within molecules or between molecules as well as in crystals. More precisely, the force field refers to the functional form and parameter sets used to calculate the potential energy of a system of the atomistic level. Force fields are usually used in molecular dynamics or Monte Carlo simulations. The parameters for a chosen energy function may be derived from classical laboratory experiment data, calculations in quantum mechanics, or both. Force fields utilize the same concept as force fields in classical physics, with the main difference that the force field parameters in chemistry describe the energy landscape on the atomistic level. From a force field, the acting forces on every particle are derived as a gradient of the potential energy with respect to the particle coordinates.
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In molecular modelling, docking is a method which predicts the preferred orientation of one molecule to another when bound together in a stable complex. In the case of protein docking, the search space consists of all possible orientations of the protein with respect to the ligand. Flexible docking in addition considers all possible conformations of the protein paired with all possible conformations of the ligand.
In biochemistry, intercalation is the insertion of molecules between the planar bases of deoxyribonucleic acid (DNA). This process is used as a method for analyzing DNA and it is also the basis of certain kinds of poisoning.
The complementarity plot (CP) is a graphical tool for structural validation of atomic models for both folded globular proteins and protein-protein interfaces. It is based on a probabilistic representation of preferred amino acid side-chain orientation, analogous to the preferred backbone orientation of Ramachandran plots). It can potentially serve to elucidate protein folding as well as binding. The upgraded versions of the software suite is available and maintained in github for both folded globular proteins as well as inter-protein complexes. The software is included in the bioinformatic tool suites OmicTools and Delphi tools.
References
- ↑ Katzir, Ephraim (2009). "Chapter 33". A Life's Tale (English language ed.). Carmel Publishing House. ISBN 978-965-540-026-7.
- ↑ Katchalski-Katzir E, Shariv I, Eisenstein M, Friesem AA, Aflalo C, Vakser IA (1992). "Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques". Proc Natl Acad Sci USA. 89 (6): 2195–2199. Bibcode:1992PNAS...89.2195K. doi: 10.1073/pnas.89.6.2195 . PMC 48623 . PMID 1549581.
- ↑ "MolFit". Weizmann Institute of Science. Retrieved 22 February 2018.
- ↑ "FTDock (v2.0)". Structural Bioinformatics Group. Retrieved 22 February 2018.
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