Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation.
about
On the characterization and software implementation of general protein lattice modelsCharacterization of protein-protein interfacesThe use of experimental structures to model protein dynamicsInsight into the structure, dynamics and the unfolding property of amylosucrases: implications of rational engineering on thermostabilityRecognizing misfolded and distorted protein structures by the assumption-based similarity score.Environment-dependent residue contact energies for proteins.Lattice protein folding with two and four-body statistical potentials.Statistical potentials for fold assessment.Database-derived potentials dependent on protein size for in silico folding and design.Protein structure evaluation using an all-atom energy based empirical scoring function.A new generation of statistical potentials for proteins.Screened nonbonded interactions in native proteins manipulate optimal paths for robust residue communication.Quantitative prediction of protein-protein binding affinity with a potential of mean force considering volume correction.New statistical potential for quality assessment of protein models and a survey of energy functionsProtein structure modelling and evaluation based on a 4-distance description of side-chain interactionsAnomalies in the vibrational dynamics of proteins are a consequence of fractal-like structureAbsolute quality evaluation of protein model structures using statistical potentials with respect to the native and reference states.NCACO-score: an effective main-chain dependent scoring function for structure modelingA beta-complex statistical four body contact potential combined with a hydrogen bond statistical potential recognizes the correct native structure from protein decoy sets.Influence of protein structure databases on the predictive power of statistical pair potentials.Exploring global motions and correlations in the ribosome.A force field for virtual atom molecular mechanics of proteinsA stochastic algorithm for global optimization and for best populations: a test case of side chains in proteins.Predicting internal protein dynamics from structures using coupled networks of hindered rotators.Coexistence of flexibility and stability of proteins: an equation of state.Elastic network model of allosteric regulation in protein kinase PDK1Towards understanding the mechanisms of molecular recognition by computer simulations of ligand-protein interactions.Herpes B virus gD interaction with its human receptor--an in silico analysis approach.Anisotropy of fluctuation dynamics of proteins with an elastic network modelSpecificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant.Relating molecular flexibility to function: a case study of tubulin.Structure-based prediction of potential binding and nonbinding peptides to HIV-1 proteaseHow similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residuesCooperativity among short amyloid stretches in long amyloidogenic sequencesAn information theoretic approach to macromolecular modeling: II. Force fieldsA tailor-made "tag-receptor" affinity pair for the purification of fusion proteins.Elastic Network Models are Robust to Variations in FormalismA novel index of protein-protein interface propensity improves interface residue recognitionIdeal architecture of residue packing and its observation in protein structures.Empirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactions
P2860
Q21133612-1F4B3F49-72BF-4046-8C1F-7C60E0903A4AQ24653393-D1264B8A-9CD6-4A4C-A546-C6C753BB699FQ28654488-3282E94D-F3CB-49DD-9560-DE4849DF39E8Q28727426-5CB5EC5D-A026-4BDB-9663-B149CB17831AQ30312666-C97ECE82-2EEB-4BB0-B3D9-A6D1D4978745Q30326368-00B763A0-E674-45EA-8B09-B7C8C5CDC892Q30328050-1D700321-7A57-4548-968D-621C257F6E4BQ30329417-168A4CF6-7718-4A48-8BA4-2CCBB49E8C3EQ30342170-EB9C4B2C-6550-4C7B-82ED-ADB8861D15C1Q30352261-6AB134C4-0A76-46E6-B625-A22A28FF4CFDQ30353364-EC17F4E5-1DE0-48AA-B0B4-657178075151Q30359796-12E07750-AC18-479A-93E2-CCDAEA2D22E6Q30381275-E2D2F37B-3BD2-4FF2-9794-7C952DD16316Q30386627-75A5FB2A-D3FE-4CB8-857C-6DCDF08CB7F2Q30391311-DBD71505-E757-474A-8732-29FA076E749CQ30391535-A5F25652-B6E1-4045-8F5D-0EF5192E5FE3Q30400320-18D86DA6-E171-4B7B-B3A7-1CCF3098CF0FQ30403122-8651512F-016D-43AF-8B4E-50D6FC04AEE7Q30429145-47F407F8-6ED8-43D2-9826-2C1DB8BC91A4Q30430527-CC8694F6-256A-43A8-B315-CB1AD9E0F612Q30476762-904D47B3-BD8D-46B7-8536-858E22FB12D4Q30489864-B9325E2F-FA72-4323-B303-0AB1D71A9172Q30797846-A245E39F-4BA5-4B26-81F5-7B1DCA537695Q33229351-B2188DFD-A107-4659-A38E-BD75C767F05BQ33509513-53AA4F55-861C-4F96-B12A-0BAFD77D85D2Q33586768-55CD898F-0AEF-4CD9-97C0-AA3FAA923C9FQ33803957-AE617810-48A2-472A-9636-BF458FF88DD5Q33930801-89A844F2-C3E3-45B8-AF3E-634333635EBCQ33931550-87947C61-90A3-4E23-B97A-09A545D6C361Q33987438-BC278CF1-CEAE-4857-84B9-984B8F4FFA65Q34178409-16706AE6-7A41-45F8-9535-D957F7827501Q34182245-3EB3780B-FCB2-4B55-9403-47E00C44F77AQ34189279-5ED08F0C-EF4F-44D2-894E-612FC376918BQ34326067-434E38A6-25AE-48A2-92EE-09C3D8FC2F3BQ34351635-2DB8CEC6-CF85-4E93-875B-09323CD411D4Q35182651-2603761C-24B9-40E0-B4B2-C3D844480E95Q36178591-BC874DA3-8C99-4043-B8A9-6CD6E474B552Q36268738-D9589337-C97F-4CC9-A35B-E67DDD2A9E22Q36280184-7FD29173-B3ED-4458-9087-6F215994B5B6Q36280764-E9956672-1B8C-4997-8C6E-600CA955671B
P2860
Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Inter-residue potentials in gl ...... eractions at close separation.
@en
Inter-residue potentials in gl ...... eractions at close separation.
@nl
type
label
Inter-residue potentials in gl ...... eractions at close separation.
@en
Inter-residue potentials in gl ...... eractions at close separation.
@nl
prefLabel
Inter-residue potentials in gl ...... eractions at close separation.
@en
Inter-residue potentials in gl ...... eractions at close separation.
@nl
P356
P1476
Inter-residue potentials in gl ...... eractions at close separation.
@en
P2093
P304
P356
10.1006/JMBI.1996.0758
P407
P577
1997-02-01T00:00:00Z