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Physicochemical Properties of Ion Pairs of Biological MacromoleculesLigands for pheromone-sensing neurons are not conformationally activated odorant binding proteinsHydrophobic Surface Burial Is the Major Stability Determinant of a Flat, Single-layer β-SheetCrystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus--structural basis of substrate recognitionSelection and Structure of Hyperactive Inteins: Peripheral Changes Relayed to the Catalytic CenterCrystal Structure of a Charge Engineered Human Lysozyme Having Enhanced Bactericidal ActivityStructural and Functional Characterization of the Kindlin-1 Pleckstrin Homology DomainSolution Structure of the QUA1 Dimerization Domain of pXqua, the Xenopus Ortholog of QuakingEnhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain ArraySerial Femtosecond Crystallography of G Protein-Coupled ReceptorsStructural analysis of trimeric phospholipase A2 neurotoxin from the Australian taipan snake venomA tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolorEnhancing zinc-finger-nuclease activity with improved obligate heterodimeric architecturesIdentification of the roles of conserved charged residues in the extracellular domain of an epithelial sodium channel (ENaC) subunit by alanine mutagenesisConformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold proteinA multiparametric computational algorithm for comprehensive assessment of genetic mutations in mucopolysaccharidosis type IIIA (Sanfilippo syndrome)Binding Interactions of Keratin-Based Hair Fiber Extract to Gold, Keratin, and BMP-2Structural characterization of the conformational change in calbindin-D28k upon calcium binding using differential surface modification analyzed by mass spectrometryPositive selection in octopus haemocyanin indicates functional links to temperature adaptationComparative Functional Genomic Analysis of Two Vibrio Phages Reveals Complex Metabolic Interactions with the Host CellActivity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family MembersDifferential Strengths of Positive Selection Revealed by Hitchhiking Effects at Small Physical Scales in Drosophila melanogasterAn intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Impact of distant charge reversals within a robust beta-barrel protein poreToward quantitative characterization of the binding profile between the human amphiphysin-1 SH3 domain and its peptide ligands.Structural Analysis of Der p 1-Antibody Complexes and Comparison with Complexes of Proteins or Peptides with Monoclonal AntibodiesSBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files.Ion pairs in non-redundant protein structures.Structural significance of the β1K396 residue found in the Porphyromonas gingivalis sialidase β-propeller domain: a computational study with implications for novel therapeutics against periodontal disease.Thermostability of in vitro evolved Bacillus subtilis lipase A: a network and dynamics perspective.Identifying stabilizing key residues in proteins using interresidue interaction energy matrix.Domain atrophy creates rare cases of functional partial protein domainsThermodynamics of antibody-antigen interaction revealed by mutation analysis of antibody variable regions.Predicting protein thermal stability changes upon point mutations using statistical potentials: Introducing HoTMuSiC.Hyperdimensional analysis of amino acid pair distributions in proteins.A method to rationally increase protein stability based on the charge-charge interaction, with application to lipase LipK107.Structure of the Triatoma virus capsidMolecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutationsMechanisms of intramolecular communication in a hyperthermophilic acylaminoacyl peptidase: a molecular dynamics investigation.Electrostatic contributions to the stability of the GCN4 leucine zipper structure.
P2860
Q26782002-67FDF3D9-BE72-42D9-B741-B8801C9A6513Q27317744-5B98FFAB-1314-43E9-837D-495B8ECF3416Q27643972-10BB513A-416E-4A6A-9165-A6E463113217Q27653471-3E5EA8F6-27D8-4CE4-A3EF-1AB59DCB9B15Q27657388-60582A21-8E55-44E0-A3B6-2A1F217D42B0Q27667276-3EC38515-CBD2-4A9C-8D97-60622DCAEF3AQ27675000-A3855DEE-ECAC-40CC-92DC-33616161F867Q27676982-DF88850F-91A6-4CA7-B060-82639A811A08Q27678660-D420FAC1-612F-410C-BEEB-AE5ECD9DE4ADQ27680992-4F6A1D5C-21EC-496D-8DF3-E92C6830CF28Q27681730-0A8A0ED9-F978-416B-BA9D-DC3D8C16F55CQ27690712-DEA03B7D-691F-4272-8BA9-E37D878FA9AEQ28299915-BAD129D9-4E00-4674-8253-5B6BA623C3E7Q28302470-D1CF4E34-183B-4D06-9ED4-E83CC319A46BQ28535095-BD5D7A20-EAA7-4445-84DA-74C6DF529F82Q28544979-29D8270D-EDCF-4E52-831F-7314FCB4F9FDQ28547606-52AEB1AB-9BFF-4588-8E1A-B3C80241BEC9Q28569218-06469609-35FB-48D0-A72F-9E53597FB38EQ28647580-3575DF32-21EC-4273-874A-573317555E69Q28821515-665604AF-3BA4-4A2C-9FA7-0E0A8FE93519Q28834252-76ACBAD1-F4DF-474E-8512-D7D781D86679Q29543946-9DAAC675-AE92-476C-AA94-C05F4A595EBFQ30153240-E10EE70B-917F-4819-A748-05ADE4D3E483Q30156821-B6B130F7-E4A4-4CD0-80AD-42CEB65BE90BQ30157169-41ACDB6A-C830-4A2D-8C31-9861434E08FAQ30279264-7BA375AE-669F-46D6-A58A-06E0DF19C048Q30361567-16FCC5B3-A8F3-4E45-9BC4-F61183FA4011Q30363935-6C038BDA-B923-4571-BD97-BCD15033580BQ30364436-931F05C5-9A5B-46D1-83AC-4B2AB8C71C20Q30365682-D7DA58D4-016A-4116-A4D2-54E0C20E9A72Q30367305-6691707A-1A0E-4631-B18C-3559B2BA2F1AQ30374251-CF757CCE-C95A-4DCA-A621-4A571FC5C97CQ30374518-3E615B3F-3B33-4214-9C53-974B8256274EQ30385777-A9F7E1BA-F1A8-4185-B69B-61EC4007270DQ30410735-9550F878-0DD2-44A7-8C95-3FB74BDC0470Q30486559-8ECFF00B-3C5F-4C12-ABBE-61E054FBF08EQ30630404-64FC4677-B194-4A3E-9F5A-416003F1FDF1Q31030886-E10FE447-6365-4A97-829B-B4D3E3BBCBE4Q31060831-8D844CDA-F96B-4F63-AA34-A88106AC443AQ31132445-3CD2EE93-9FB7-42F3-8455-54A7E1045DF8
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Close-range electrostatic interactions in proteins
@ast
Close-range electrostatic interactions in proteins
@en
Close-range electrostatic interactions in proteins
@nl
type
label
Close-range electrostatic interactions in proteins
@ast
Close-range electrostatic interactions in proteins
@en
Close-range electrostatic interactions in proteins
@nl
prefLabel
Close-range electrostatic interactions in proteins
@ast
Close-range electrostatic interactions in proteins
@en
Close-range electrostatic interactions in proteins
@nl
P3181
P1433
P1476
Close-range electrostatic interactions in proteins
@en
P2093
Sandeep Kumar
P304
P3181
P356
10.1002/1439-7633(20020703)3:7<604::AID-CBIC604>3.0.CO;2-X
P407
P577
2002-07-02T00:00:00Z