Physical reasons for the unusual alpha-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides - Wikidata - awgldk - TriplyDB

Physical reasons for the unusual alpha-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides

Physical reasons for the unusual alpha-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides

http://www.wikidata.org/entity/Q37281519

about

Solvent effect on the folding dynamics and structure of E6-associated protein characterized from ab initio protein folding simulations.The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR.Helix formation via conformation diffusion search A closer look into the α-helix basin.The alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation.Alpha-helical stabilization by side chain shielding of backbone hydrogen bonds.On the role of the SP1 domain in HIV-1 particle assembly: a molecular switch?Conformation, orientation, and adsorption kinetics of dermaseptin B2 onto synthetic supports at aqueous/solid interface Atomically detailed simulations of helix formation with the stochastic difference equation Role of backbone hydration and salt-bridge formation in stability of alpha-helix in solution.Exploring the helix-coil transition via all-atom equilibrium ensemble simulations Water's role in the force-induced unfolding of ubiquitin.Geometry and symmetry presculpt the free-energy landscape of proteins Solvent effects on the energy landscapes and folding kinetics of polyalanine.Insufficiently dehydrated hydrogen bonds as determinants of protein interactions Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis.Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide.In search of the energetic role of peptide hydrogen bonds.Secondary structure provides a template for the folding of nearby polypeptides.The cPLA2 C2alpha domain in solution: structure and dynamics of its Ca2+-activated and cation-free states Lysine and arginine residues do not increase the helicity of alanine-rich peptide helices.Conformational sampling of peptides in cellular environments.Protein-solvent interactions Dynamic charge interactions create surprising rigidity in the ER/K alpha-helical protein motif.Conformational Properties of Helical Protein Polymers with Varying Densities of Chemically Reactive Groups Conformational behavior of chemically reactive alanine-rich repetitive protein polymers.Structural insights for designed alanine-rich helices: comparing NMR helicity measures and conformational ensembles from molecular dynamics simulation Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures.Thermodynamics of alpha- and beta-structure formation in proteins.Folding thermodynamics of peptides.Potentials of mean force for the interaction of blocked alanine dipeptide molecules in water and gas phase from MD simulations Solvent effects on the conformational transition of a model polyalanine peptide.Salt dependence of an alpha-helical peptide folding energy landscapes.An alpha-helical peptide in AOT micelles prefers to be localized at the water/headgroup interface.Automated Optimization of Potential Parameters.Polymorphism, shared functions and convergent evolution of genes with sequences coding for polyalanine domains.Molecular dynamics study of an insertion/duplication mutant of bacteriophage T4 lysozyme reveals the nature of α→β transition in full protein context.Comparison of hydration behavior and conformational preferences of the Trp-cage mini-protein in different rigid-body water models.Communication: The electrostatic polarization is essential to differentiate the helical propensity in polyalanine mutants.A direct multiple histogram reweighting method for optimal computation of the density of states.

P2860

Q30415112-92A1CA4A-6A75-4ED0-8B71-C91FDF2DDD26 Q30769903-497F8C1F-64F5-48A6-BD63-C11A42B9EC5A Q30819952-6370E00F-0BC0-4A65-9EDC-835546AECE42 Q30830738-FB50C6F1-451B-4574-9109-E978D96383F5 Q30984765-BB13D194-7FC9-4859-8FCA-08371F53D272 Q34014321-212D2DA4-1F4D-4DBA-9500-8629FD555A28 Q34164929-584CFACF-3649-41E9-9D1D-31FE5BA61840 Q34182358-4432CB80-BAF7-4897-B696-6507B09790FF Q34183483-19C030B0-00F9-41BF-B935-F40AD41B9596 Q34183582-860CFD9F-415A-44BF-9CD8-2917BE7C73BC Q34189691-A0304C63-B1C2-4A60-B41E-1A73C55AC64A Q34320534-0AB78E4D-3057-4F54-8B03-FA21CD2A5349 Q34330691-37118C99-092B-4B57-AE55-689CD1FBCFF1 Q34445434-9EDDAD56-9991-4081-9C3E-61AAFE89B471 Q34466734-691E8243-469C-4BEE-AD39-8E15B7C4C4A8 Q34805610-D833A9DB-FD99-4153-BD1B-6C7D27C50501 Q34984717-BEC4EA01-F153-4872-ACCF-A184D73BBDC6 Q35064700-17B80C32-D2A3-4273-9C91-F97FC13AA96D Q35215030-0AAC4BF0-752D-407E-AE63-AFD976B0BB00 Q35606778-DC8FD857-9B26-4558-88A1-267249E15F5A Q35607904-C7A82688-5677-4951-B13D-0E247104592C Q36344939-4B50D361-323C-4A3C-B2B0-5D1E22A43B2D Q36472761-4B2E95D9-5299-4632-8D14-49DD10E0AD00 Q36869856-1CD0FCD1-CEAD-45D8-9764-A731CF29029A Q37076699-0608E15E-270E-452B-AE19-E2396C20DBEA Q37115367-883969D3-4461-4C4C-AC70-A0DAFEBA5B09 Q37275705-D50BA6C1-3EF9-48BE-9B44-9713C7881620 Q40216639-810BA9D9-7CDA-4E0B-BC31-1B49EC5C5AFD Q40251298-BE5B7F77-BBFC-4CDE-A1EF-1DAAE5974FA3 Q40319333-2EDA05CB-329D-4780-813B-67D5DFF5DD01 Q41824624-E766A1B4-418E-4F42-8F15-388637CFE64F Q42037889-DAA1367F-9360-43F2-9CDF-65B0F479959C Q42411748-4C50D952-410D-491C-BAFB-00A36F1DDEF7 Q42538477-45C2C7FF-B045-4546-95F0-D7A4919B657B Q42586074-8FA96E00-A8DC-43D9-B138-23683DA1E072 Q42609875-4CF30607-D36F-4135-B51E-5ED30E9E1EB3 Q51061591-4750551E-E28D-44DE-B21D-0BAB718DF5F9 Q51309269-CE47AD6D-E892-4C3C-8389-DA8F6F4082B5 Q51571593-DCE9D9A4-F3F2-4F5D-9FA0-F4FC0C6A8B44 Q51618942-99D3280A-1FAC-43AE-B20A-7D826657D558

P2860

Physical reasons for the unusual alpha-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides

http://www.wikidata.org/entity/Q37281519

description

2000 nî lūn-bûn

@nan

2000年の論文

@ja

2000年学术文章

@wuu

2000年学术文章

@zh-cn

2000年学术文章

@zh-hans

2000年学术文章

@zh-my

2000年学术文章

@zh-sg

2000年學術文章

@yue

2000年學術文章

@zh

2000年學術文章

@zh-hant

name

Physical reasons for the unusu ...... idues in alanine-rich peptides

@en

Physical reasons for the unusu ...... dues in alanine-rich peptides.

@nl

type

label

Physical reasons for the unusu ...... idues in alanine-rich peptides

@en

Physical reasons for the unusu ...... dues in alanine-rich peptides.

@nl

prefLabel

Physical reasons for the unusu ...... idues in alanine-rich peptides

@en

Physical reasons for the unusu ...... dues in alanine-rich peptides.

@nl

P1433

Q37281519-AAAD4290-BBCC-4FCF-B330-72729501480A

P1476

Q37281519-08C265EF-B41B-445F-91E6-F464EF1226D8

P2093

Q37281519-95ABE6F6-2C46-483D-AE9F-A4CD389E90D6

Q37281519-F36D3187-BB1E-499D-9F95-E9AF6E0FEB8B

P2860

Q37281519-3638C5E8-8AC7-4262-ACB9-58475D9AD35C

Q37281519-53CFD026-3AA3-45E8-9256-A24C6AF8C293

Q37281519-5E5481F3-5780-4404-9CBB-B2220D368EB6

Q37281519-637D1B9D-62CE-40B9-8BAC-654B6FED4A9F

Q37281519-79160F35-B472-445E-A90C-E97A8A87C5EE

Q37281519-8FEE7CE3-593F-4C3B-B476-ABA4AE895E18

Q37281519-B1B0C49E-084D-40E4-817E-CB7AF581EEC3

Q37281519-B358F634-142F-468F-8CD0-FA77185FE138

Q37281519-F3EF73F9-7BB4-46B1-8162-4524915401B9

P304

Q37281519-C12F6ADA-23B1-41DB-B6A6-487937963739

P31

Q37281519-87EDA8AB-92EC-4774-AE57-7FA0E354B578

P356

Q37281519-8133E892-0E27-483A-A361-6889A9620460

P407

Q37281519-D0631CB3-6072-4A33-8A48-7EBA2DE91FFB

P433

Q37281519-6D85EA28-2CEC-43FA-AFF5-544263EB22C0

P478

Q37281519-8FC03FFE-998C-4AAF-B472-747F8CB3861E

P50

Q37281519-82A2F200-6E69-4174-B0EF-F63FDAC2DEF8

P577

Q37281519-867C473C-6AD2-4AD5-94E7-012F9FE77353

P5875

Q37281519-E9306A61-F818-42E5-BE22-9348364196B8

P698

Q37281519-E2C36FB3-92F2-48FD-B928-873EA2B21987

P932

Q37281519-EB9A03A7-1545-40C9-89A8-9A025E59F3D2

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Physical reasons for the unusu ...... idues in alanine-rich peptides

@en

P2093

D R Ripoll

http://www.w3.org/2001/XMLSchema#string

J A Vila

http://www.w3.org/2001/XMLSchema#string

P2860

Unusually stable helix formation in short alanine-based peptides

Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol.

The intrinsic helix-forming tendency of L-alanine.

Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities.

On the pH-conformational dependence of the unblocked SYPYD peptide.

Coupling between folding and ionization equilibria: effects of pH on the conformational preferences of polypeptides.

Conformational studies of poly-L-alanine in water.

Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains

Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol

P304

13075-13079

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.240455797

http://www.w3.org/2001/XMLSchema#string

P407

P433

24

http://www.w3.org/2001/XMLSchema#string

P478

97

http://www.w3.org/2001/XMLSchema#string

P50

Harold A. Scheraga

P577

2000-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12248270

http://www.w3.org/2001/XMLSchema#string

P698

11078529

http://www.w3.org/2001/XMLSchema#string

P932

27180

http://www.w3.org/2001/XMLSchema#string