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Improved Chou-Fasman method for protein secondary structure predictionExploring steric constraints on protein mutations using MAGE/PROBEEngineering therapeutic antibodies targeting G-protein-coupled receptorsStructural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein foldingStructure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein designStructural consequences of replacement of an alpha-helical Pro residue in Escherichia coli thioredoxinUnique stabilizing interactions identified in the two-stranded α-helical coiled-coil: Crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptideStructural characterization of human S100A16, a low-affinity calcium binderMechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor DomainsAre the parameters of various stabilization factors estimated from mutant human lysozymes compatible with other proteins?The yeast mitochondrial citrate transport protein. Probing the roles of cysteines, Arg(181), and Arg(189) in transporter functionA knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding.Folding of proteins with an all-atom Go-model.Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure.Sequence periodicity and secondary structure propensity in model proteins.A RASSF1A polymorphism restricts p53/p73 activation and associates with poor survival and accelerated age of onset of soft tissue sarcoma.A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.Site-specific incorporation of biophysical probes into proteins.A solvent model for simulations of peptides in bilayers. I. Membrane-promoting alpha-helix formationFactors important for fusogenic activity of peptides: molecular modeling study of analogs of fusion peptide of influenza virus hemagglutinin.Helix-stabilizing effects of the pentapeptide KIFMK and its related peptides on the sodium channel inactivation gate peptides.Investigating and Engineering Enzymes by Genetic Selection.An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper.Domain motions in bacteriophage T4 lysozyme: a comparison between molecular dynamics and crystallographic data.Correlation between amino acid residues converted by RNA editing and functional residues in protein three-dimensional structures in plant organellesInvestigation of the three-dimensional architecture of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans by electron tomography.Position-specific propensities of amino acids in the β-strand.Statistical analysis and molecular dynamics simulations of ambivalent α-helices.The activated state of a sodium channel voltage sensor in a membrane environmentA putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assemblyRelationship between side chain structure and 14-helix stability of beta3-peptides in waterHydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha-helices.Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides.Dependence of α-helical and β-sheet amino acid propensities on the overall protein fold type.The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.Mutational analysis of the [Het-s] prion analog of Podospora anserina. A short N-terminal peptide allows prion propagationHelical ambivalency induced by point mutations.The accessory helix of complexin functions by stabilizing central helix secondary structureEffect of the peptide secondary structure on the peptide amphiphile supramolecular structure and interactions.Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin.
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Structural basis of amino acid alpha helix propensity
@ast
Structural basis of amino acid alpha helix propensity
@en
Structural basis of amino acid alpha helix propensity
@nl
type
label
Structural basis of amino acid alpha helix propensity
@ast
Structural basis of amino acid alpha helix propensity
@en
Structural basis of amino acid alpha helix propensity
@nl
prefLabel
Structural basis of amino acid alpha helix propensity
@ast
Structural basis of amino acid alpha helix propensity
@en
Structural basis of amino acid alpha helix propensity
@nl
P2093
P356
P1433
P1476
Structural basis of amino acid alpha helix propensity
@en
P2093
P304
P356
10.1126/SCIENCE.8503008
P407
P577
1993-06-11T00:00:00Z