The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
about
The role of hydrophobic interactions in positioning of peripheral proteins in membranesInteratomic potentials and solvation parameters from protein engineering data for buried residuesModels for the 3(10)-helix/coil, pi-helix/coil, and alpha-helix/3(10)-helix/coil transitions in isolated peptidesCrystal structure of the hyperthermophilic inorganic pyrophosphatase from the archaeon Pyrococcus horikoshiiThe structure, molecular dynamics, and energetics of centrin-melittin complexEnhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain ArrayStructural and Functional Characterization of a Complex between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 Subunit of TFIIHDetermination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructsGlobal perspectives on proteins: comparing genomes in terms of folds, pathways and beyond.Compositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.Stimuli responsive deswelling of radiation synthesized collagen hydrogel in simulated physiological environment.Helix-stabilizing effects of the pentapeptide KIFMK and its related peptides on the sodium channel inactivation gate peptides.Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor.Sequence dependence of beta-hairpin structure: comparison of a salt bridge and an aromatic interaction.Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles.The effect of charge-charge interactions on the kinetics of alpha-helix formation.Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites.Critical interactions in the stability control region of tropomyosin.A thermodynamic model for the helix-coil transition coupled to dimerization of short coiled-coil peptides.Hydrogen bonding stabilizes globular proteins.Backbone dipoles generate positive potentials in all proteins: origins and implications of the effectSalt effects on ionization equilibria of histidines in myoglobinMolecular dynamics simulations of wild-type and mutant forms of the Mycobacterium tuberculosis MscL channelMultivalent protein polymers with controlled chemical and physical properties.The effects of pK(a) tuning on the thermodynamics and kinetics of folding: design of a solvent-shielded carboxylate pair at the a-position of a coiled-coilMarburg virus glycoprotein GP2: pH-dependent stability of the ectodomain α-helical bundlePrediction of polyelectrolyte polypeptide structures using Monte Carlo conformational search methods with implicit solvation modeling.Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol.The turn sequence directs beta-strand alignment in designed beta-hairpins.Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteinsAlanine is helix-stabilizing in both template-nucleated and standard peptide helicesEffect of the N3 residue on the stability of the alpha-helix.Osmolyte effects on helix formation in peptides and the stability of coiled-coilsCharged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone chargesEvaluation of conformation and association behavior of multivalent alanine-rich polypeptides.Conformational Properties of Helical Protein Polymers with Varying Densities of Chemically Reactive GroupsArchitecture Effects on the Binding of Cholera Toxin by Helical Glycopolypeptides.Conformational behavior of chemically reactive alanine-rich repetitive protein polymers.
P2860
Q21093294-F8BBE6D6-8955-4B11-BD68-555606D54B27Q24644861-6723F4F5-3B78-4100-A85C-88EF685A38B4Q24673823-64D5EF5E-F4D8-465D-8D82-38737EB0896AQ27642851-5A23A225-BB37-48FE-945C-155E0EEA9896Q27674964-2E19AA46-4045-44D9-84CA-702E6F867DAEQ27678660-8202F2F3-360D-4396-9B26-B998F86EA79DQ27682610-9745B4E9-5E58-4453-8000-D6CA9C88D7B7Q27732838-C85BAA12-2A49-4617-BF87-C9D2EAC17068Q30330015-F5808A6E-8CB2-4A0A-9073-94A46B481219Q30402003-F60585BE-7590-459E-858E-F237BC7D620DQ30420444-21F66898-15B6-4D3F-875F-C4F226B36DD1Q30580694-AD2F3D71-90AD-4558-91FD-1E5C5E021F91Q30583940-ED43D946-9A2C-4D50-815D-C6AE732313F0Q30679573-054AC133-B4DD-43C8-9CD7-41D7F49A861EQ30977526-8DD3A7D4-3E8E-47C2-95D0-86A1D80ADF4DQ33195172-7FD95C92-95EE-45D0-9A6B-422FA944092CQ33280503-073EE88C-FFB7-4264-A5A3-10363820BB6AQ33294390-C3E29632-C593-4170-8178-6A680778557BQ33638911-64C2B830-97BD-4EAA-83E2-C77C3D006DB8Q33798510-0204CA85-DAC2-4505-A92C-A905F4D50115Q34018251-66AA12C2-F2D8-4276-94EA-817831917F6FQ34040782-062063C7-E974-49D6-BE07-54517417E46AQ34172536-C210C21F-DEFF-4E30-8F83-9F4F4294A408Q34173934-DCACCDFB-8218-43F3-876F-762C0230CC84Q34176308-D037F5FF-77D1-4875-A9F1-9B3D32857C46Q34514739-22F5DD30-3B6E-450B-8B2F-5368AACCFBD7Q34590625-3033837A-DCFE-4BDB-809D-73CBD182982CQ35857049-E73F3943-91BC-44B7-A303-08ADE1736856Q36278931-F07B8802-C629-4598-B7EF-635757C62D88Q36279587-54625AC9-605B-4A60-A7B7-85F760580421Q36281322-8639BB15-8DF8-4991-98E4-921FC878C213Q36331997-4820B317-6A18-40B0-BA4A-7C5A367FB60EQ36448925-2C6E1AF5-57D7-4D48-A36A-510429494E95Q36526189-9CC6764E-FEA0-4396-9C90-CBB89BC996F7Q36639484-0C574E35-A608-4E84-AD2C-0EF738649650Q36702071-7E208F22-8E87-49A7-B563-A926AEF8ECDEQ37076671-C8045837-2E9C-403B-BA5E-3F95204AD3EAQ37076699-76517A92-EB2E-4EB7-BFBE-A0A4CDEB6604Q37091452-B42C5F2C-BF96-4F54-B2E0-7F3E3FAE57B3Q37115367-EE5E8A05-04E3-47AD-AD48-522295101589
P2860
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@en
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@nl
type
label
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@en
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@nl
prefLabel
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@en
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@nl
P2093
P356
P1433
P1476
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.
@en
P2093
P304
P356
10.1021/BI00088A019
P407
P577
1993-09-01T00:00:00Z