A survey of left-handed polyproline II helices

scientific article

A survey of left-handed polyproline II helices is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1110/PS.8.3.587
P932PMC publication ID2144280
P698PubMed publication ID10091661
P5875ResearchGate publication ID227637564

P2093author name stringCreamer TP
Stapley BJ
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N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptidesQ24675075
Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactionsQ27729407
The 2.0-A resolution structure of soybean beta-amylase complexed with alpha-cyclodextrinQ27731953
Crystallographic refinement of lignin peroxidase at 2 AQ27732094
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Crystal structure of the Src family tyrosine kinase HckQ27734750
The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide bindingQ27746689
Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulationQ27747144
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical featuresQ27860675
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Amino acid preferences for specific locations at the ends of alpha helicesQ29618508
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide.Q30176860
Helix signals in proteinsQ30400745
Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical modelsQ33396768
Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptidesQ33575103
Chain conformation in the collagen moleculeQ34213877
Conformational analysis of the backbone-dependent rotamer preferences of protein sidechainsQ34304282
Enlarged representative set of protein structuresQ36278475
The role of PII conformations in the calculation of peptide fractional helix contentQ36280554
Role of the C-terminal region of beta-amylase from barleyQ39617407
TonB protein of Salmonella typhimurium. A model for signal transduction between membranesQ42106091
Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structuresQ47631461
Influence of proline residues on protein conformationQ47638868
Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.Q52364819
Left-handed polyproline II helices commonly occur in globular proteins.Q52402236
Analysis of the relationship between side-chain conformation and secondary structure in globular proteinsQ68541264
P433issue3
P1104number of pages9
P304page(s)587-595
P577publication date1999-03-01
P1433published inProtein ScienceQ7251445
P1476titleA survey of left-handed polyproline II helices
P478volume8

Reverse relations

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