scholarly journals Characterization of Ionizable Groups’ Environments in Proteins and Protein–Ligand Complexes through a Statistical Analysis of the Protein Data Bank

ACS Omega ◽  
2017 ◽  
Vol 2 (10) ◽  
pp. 7359-7374
Author(s):  
Alexandre Borrel ◽  
Anne-Claude Camproux ◽  
Henri Xhaard
Keyword(s):  
Statistical Analysis ◽  
Protein Data Bank ◽  
Data Bank ◽  
Ionizable Groups

scholarly journals Disordered Residues and Patterns in the Protein Data Bank

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1522 ◽  
Author(s):  
Mikhail Yu. Lobanov ◽  
Ilya V. Likhachev ◽  
Oxana V. Galzitskaya
Keyword(s):  
Amino Acids ◽  
Statistical Analysis ◽  
Protein Data Bank ◽  
Protein Structures ◽  
3D Structure ◽  
Data Bank ◽  
Disordered Regions

We created a new library of disordered patterns and disordered residues in the Protein Data Bank (PDB). To obtain such datasets, we clustered the PDB and obtained the groups of chains with different identities and marked disordered residues. We elaborated a new procedure for finding disordered patterns and created a new version of the library. This library includes three sets of patterns: unique patterns, patterns consisting of two kinds of amino acids, and homo-repeats. Using this database, the user can: (1) find homologues in the entire Protein Data Bank; (2) perform a statistical analysis of disordered residues in protein structures; (3) search for disordered patterns and homo-repeats; (4) search for disordered regions in different chains of the same protein; (5) download clusters of protein chains with different identity from our database and library of disordered patterns; and (6) observe 3D structure interactively using MView. A new library of disordered patterns will help improve the accuracy of predictions for residues that will be structured or unstructured in a given region.

scholarly journals Statistical Analysis of the Internal Distances of Helical Pairs in Protein Molecules

2016 ◽  
Vol 11 (2) ◽  
pp. 170-190 ◽  
Author(s):  
Д.А. Тихонов ◽  
D.A. Tikhonov
Keyword(s):  
Regression Analysis ◽  
Statistical Analysis ◽  
Protein Data Bank ◽  
Long Range ◽  
Data Bank ◽  
Interplanar Distance ◽  
Minimal Distance ◽  
Gamma Distributions ◽  
Protein Molecules ◽  
Plane Passing

The statistical analysis of interhelical distances in pairs of connected α-helices found in known proteins has been performed. In accordance with the certain rules, a database of the pairs found in the Protein Data Bank has been compiled. This set was subdivided into three subsets according to criterion of crossing helix projections on the parallel plane passing through the axis of the helix. It was shown that the distribution of distances between the pairs of helices whose projections are not crossed has a more long-range nature than those whose projections are overlapped. Using the regression analysis the nature of distributions is investigated. In particular, it is shown that the distributions of interhelical distances in the subset of pairs of helices without intersections belong to the gamma distributions. It is also shown that the subset of the pairs with crossing projections have a smaller ratio of the minimal distance between the helical axes to the interplanar distance that is contrast to the set without crossing projections. It was concluded that the helical pairs with crossing projections are additionally stabilized by internal interactions.

scholarly journals The study of interhelical angles in the structural motifs formed by two helices

2017 ◽  
Vol 12 (1) ◽  
pp. 83-101 ◽  
Author(s):  
Д.А. Тихонов ◽  
D.A. Tikhonov
Keyword(s):  
Statistical Analysis ◽  
Protein Data Bank ◽  
Entire Range ◽  
Structural Organization ◽  
Protein Structures ◽  
Data Bank ◽  
Acute Angle ◽  
Spatial Structures ◽  
Pass Through ◽  
Selection Of

In this paper a statistical analysis of distributions of inter-helical angles in pairs of consecutive and connected α-helices in spatial structures of proteins is presented. A number of rules for selection of the helical pairs from a set of protein structures obtained from the Protein Data Bank (PDB) were developed. The set of helical pairs has been analyzed for the purpose of classification and finding out the features of protein structural organization. All pairs of connected helices were divided into three subsets according to the criterion of crossing of projections of the helices on parallel planes, which pass through the axes of the helices. It is shown that the distribution of all types of helical pairs, whose projections do not cross each others, covers almost the entire range of inter-helical angles. The distribution have a single maximum which is close to right angle. Most pairs in this set constitute helical pairs consisting of α- and 310-helices, and most pairs with the crossing projections of helices are helical pairs formed by two α-helices. It is also shown that a great amount of the pairs of connected α-helices has acute angle 20° ≤ φ ≤ 60° between the axes of the helices. The distribution of all types of helical pairs depending on the length of the inter-helical connections was also analyzed. It is shown that the structures with short connections occur most often in all the subsets.

scholarly journals Characteristics of Interactions at Protein Segments External to Globular Domains in the Protein Data Bank

2018 ◽  
Author(s):  
Kota Kasahara ◽  
Shintaro Minami ◽  
Yasunori Aizawa
Keyword(s):  
Amino Acid ◽  
Protein Data Bank ◽  
Protein Function ◽  
Three Dimensional ◽  
Data Bank ◽  
Side Chain ◽  
Globular Domain ◽  
Amino Acid Residues ◽  
Structural Elements

ABSTRACTThe principle of three-dimensional protein structure formation is a long-standing conundrum in structural biology. A globular domain of a soluble protein is formed by a network of atomic contacts among amino acid residues, but regions external to globular domains, like loop and linker, often do not have intramolecular contacts with globular domains. Although these regions can play key roles for protein function as interfaces for intermolecular interactions, their nature remains unclear. Here, we termed protein segments external to globular domains as floating segments and sought for them in tens of thousands of entries in the Protein Data Bank. As a result, we found that 0.72 % of residues are in floating segments. Regarding secondary structural elements, coil structures are enriched in floating segments, especially for long segments. Interactions with polypeptides and polynucleotides, but not small compounds, are enriched in floating segments. The amino acid preferences of floating segments are similar to those of surface residues, with exceptions; the small side chain amino acids, Gly and Ala, are preferred, and some charged side chains, Arg and His, are disfavored for floating segments compared to surface residues. Our comprehensive characterization of floating segments may provide insights into understanding protein sequence-structure-function relationships.

scholarly journals The Protein Data Bank: data distribution and query functionality

2002 ◽  
Vol 58 (s1) ◽  
pp. c214-c214
Author(s):  
W. F. Bluhm ◽  
T. Battistuz ◽  
E. Clingman ◽  
N. Deshpande ◽  
W. Fleri ◽  
...  
Keyword(s):  
Protein Data Bank ◽  
Data Distribution ◽  
Data Bank
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