Structure-based prediction of protein-protein binding affinity with consideration of allosteric effect.

Structure-based prediction of protein-protein binding affinity with consideration of allosteric effect.

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http://www.wikidata.org/entity/Q51496556
Mutatomics analysis of the systematic thermostability profile of Bacillus subtilis lipase A.The scoring of poses in protein-protein docking: current capabilities and future directionsMinimalistic predictor of protein binding energy: contribution of solvation factor to protein binding.How structure defines affinity in protein-protein interactions.The selectivity and promiscuity of brain-neuroregenerative inhibitors between ROCK1 and ROCK2 isoforms: An integration of SB-QSSR modelling, QM/MM analysis and in vitro kinase assay.On the binding affinity of macromolecular interactions: daring to ask why proteins interact.An unexpected way forward: towards a more accurate and rigorous protein-protein binding affinity scoring function by eliminating terms from an already simple scoring function.Computational Approaches for Predicting Binding Partners, Interface Residues, and Binding Affinity of Protein-Protein Complexes.Molecular design and genetic optimization of antimicrobial peptides containing unnatural amino acids against antibiotic-resistant bacterial infections.Contacts-based prediction of binding affinity in protein-protein complexes.On the mechanisms of protein interactions: predicting their affinity from unbound tertiary structures.Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.The critical aggregation concentration of peptide surfactants is predictable from dynamic hydrophobic property.Feature selection and classification of protein-protein complexes based on their binding affinities using machine learning approaches.Biomacromolecular quantitative structure-activity relationship (BioQSAR): a proof-of-concept study on the modeling, prediction and interpretation of protein-protein binding affinity.Streptococcus pneumoniae Genome-wide Identification and Characterization of BOX Element-binding Domains.The small-molecule inhibitor selectivity between IKKα and IKKβ kinases in NF-κB signaling pathway.
P2860

Structure-based prediction of protein-protein binding affinity with consideration of allosteric effect.

Item
http://www.wikidata.org/entity/Q51496556
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
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2011年學術文章
@zh-hant
name
Structure-based prediction of ...... deration of allosteric effect.
@en
Structure-based prediction of ...... deration of allosteric effect.
@nl
type
label
Structure-based prediction of ...... deration of allosteric effect.
@en
Structure-based prediction of ...... deration of allosteric effect.
@nl
prefLabel
Structure-based prediction of ...... deration of allosteric effect.
@en
Structure-based prediction of ...... deration of allosteric effect.
@nl
P1433
P1476
P2093
P2860
P2888
P304
P31
P356
P433
P478
P577
P698
P921
P356
P1433
P1476
Structure-based prediction of ...... deration of allosteric effect.
@en
P2093
P2860
P2888
P304
P31
P356
P433
P478
P577
P698
P921