(Q45963927)

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Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy.

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scholarly article

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy. (English)

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

computational biology

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based on heuristic

inferred from title

1

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

2

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

3

object named as

Ozlem Keskin

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

language of work or name

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publication date

8 April 2009

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

number of pages

8

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inferred from page(s)

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

25

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

12

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

1513-1520

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

Prediction of protein-protein interactions by combining structure and sequence conservation in protein interfaces

1 reference

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Anatomy of hot spots in protein interfaces

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Statistical analysis and prediction of protein-protein interfaces

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Analysis of homodimeric protein interfaces by graph-spectral methods.

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Predicting protein interaction sites: binding hot-spots in protein-protein and protein-ligand interfaces.

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Evolutionary rate in the protein interaction network

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Structure-based method for analyzing protein-protein interfaces

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The subunit interfaces of oligomeric enzymes are conserved to a similar extent to the overall protein sequences

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Identification of hot-spot residues in protein-protein interactions by computational docking

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Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

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Conservation and relative importance of residues across protein-protein interfaces

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HotSprint: database of computational hot spots in protein interfaces

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Computational alanine scanning of the 1:1 human growth hormone-receptor complex

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Structure-derived potentials and protein simulations

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21 January 2018

Hot regions in protein--protein interactions: the organization and contribution of structurally conserved hot spot residues

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21 January 2018

Empirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactions

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A simple physical model for binding energy hot spots in protein-protein complexes

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Protein-protein interactions: hot spots and structurally conserved residues often locate in complemented pockets that pre-organized in the unbound states: implications for docking

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Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A

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Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces

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21 January 2018

Hot spots--a review of the protein-protein interface determinant amino-acid residues

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Protein-protein interaction hotspots carved into sequences

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PRISM: protein interactions by structural matching

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Prediction of functional sites by analysis of sequence and structure conservation

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Force fields for protein simulations

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Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues.

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Anchor residues in protein-protein interactions

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Prediction of protein secondary structure at better than 70% accuracy

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Database of homology-derived protein structures and the structural meaning of sequence alignment

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Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins.

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Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins

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ASEdb: a database of alanine mutations and their effects on the free energy of binding in protein interactions

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Identifiers

10.1093/BIOINFORMATICS/BTP240

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

DBLP publication ID

journals/bioinformatics/TuncbagGK09

1 reference

DBLP Dataset 2021-01-02

28 January 2021

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/19357097

ResearchGate publication ID

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