scholarly article | Q13442814 |
P2093 | author name string | Creamer TP | |
Stapley BJ | |||
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Complete amino acid sequence of amelogenin in developing bovine enamel | Q71384780 | ||
Residual structure in unfolded proteins revealed by Raman optical activity | Q71571728 | ||
Structural requirements and thermodynamics of the interaction of proline peptides with profilin | Q71955434 | ||
New chain conformations of poly(glutamic acid) and polylysine | Q72087427 | ||
Poly(pro)II helices in globular proteins: identification and circular dichroic analysis | Q72130288 | ||
Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy | Q72252494 | ||
The structure and function of proline-rich regions in proteins | Q24528663 | ||
Structures of N-termini of helices in proteins | Q24673742 | ||
N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptides | Q24675075 | ||
Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions | Q27729407 | ||
The 2.0-A resolution structure of soybean beta-amylase complexed with alpha-cyclodextrin | Q27731953 | ||
Crystallographic refinement of lignin peroxidase at 2 A | Q27732094 | ||
Three-dimensional structure of the tyrosine kinase c-Src | Q27734749 | ||
Crystal structure of the Src family tyrosine kinase Hck | Q27734750 | ||
The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding | Q27746689 | ||
Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation | Q27747144 | ||
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features | Q27860675 | ||
Protein modules and signalling networks | Q27860694 | ||
Satisfying hydrogen bonding potential in proteins | Q27860940 | ||
The Protein Data Bank: a computer-based archival file for macromolecular structures | Q27860989 | ||
The SNF5 protein of Saccharomyces cerevisiae is a glutamine- and proline-rich transcriptional activator that affects expression of a broad spectrum of genes | Q27930788 | ||
Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes | Q28305615 | ||
Amino acid preferences for specific locations at the ends of alpha helices | Q29618508 | ||
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. | Q30176860 | ||
Helix signals in proteins | Q30400745 | ||
Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models | Q33396768 | ||
Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides | Q33575103 | ||
Chain conformation in the collagen molecule | Q34213877 | ||
Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains | Q34304282 | ||
Enlarged representative set of protein structures | Q36278475 | ||
The role of PII conformations in the calculation of peptide fractional helix content | Q36280554 | ||
Role of the C-terminal region of beta-amylase from barley | Q39617407 | ||
TonB protein of Salmonella typhimurium. A model for signal transduction between membranes | Q42106091 | ||
Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures | Q47631461 | ||
Influence of proline residues on protein conformation | Q47638868 | ||
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 proteins | Q68541264 | ||
P433 | issue | 3 | |
P1104 | number of pages | 9 | |
P304 | page(s) | 587-595 | |
P577 | publication date | 1999-03-01 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | A survey of left-handed polyproline II helices | |
P478 | volume | 8 |
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