Influence of proline residues on protein conformation.
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[1] P J Flory,et al. Conformational energies and configurational statistics of copolypeptides containing L-proline. , 1968, Journal of molecular biology.
[2] H. Scheraga,et al. Chain reversals in proteins. , 1973, Biochimica et biophysica acta.
[3] K. Wüthrich,et al. A novel approach for studies of the molecular conformations in flexible polypeptides , 1974, FEBS letters.
[4] P. Y. Chou,et al. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. , 1974, Biochemistry.
[5] T. Ashida,et al. The crystal structure of t‐amyloxycarbonyl‐l‐prolyl‐l‐prolyl‐l‐proline , 1974 .
[6] H. Halvorson,et al. Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. , 1975, Biochemistry.
[7] G. N. Ramachandran,et al. An explanation for the rare occurrence of cis peptide units in proteins and polypeptides. , 1976, Journal of molecular biology.
[8] H. Scheraga,et al. Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP. , 1977, Macromolecules.
[9] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[10] M. Levitt. Conformational preferences of amino acids in globular proteins. , 1978, Biochemistry.
[11] T. A. Jones,et al. A graphics model building and refinement system for macromolecules , 1978 .
[12] K. Wüthrich,et al. Conformational energy studies of linear dipeptides H‐X‐L‐Pro‐OH , 1979 .
[13] K. Wüthrich,et al. Nmr studies of the rates of proline cis–trans isomerization in oligopeptides , 1981 .
[14] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[15] C. Chothia,et al. Orthogonal packing of beta-pleated sheets in proteins. , 1982, Biochemistry.
[16] P Argos,et al. Amino acid distribution in protein secondary structures. , 2009, International journal of peptide and protein research.
[17] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[18] J. Weber,et al. Structure of the gene encoding the immunodominant surface antigen on the sporozoite of the human malaria parasite Plasmodium falciparum. , 1984, Science.
[19] T. Hofmann,et al. Basic proline-rich proteins from human parotid saliva: complete covalent structures of proteins IB-1 and IB-6. , 1986, Biochemistry.
[20] A novel supersecondary structure in globular proteins comprising the collagen-like helix and beta-turn. , 1987, Journal of molecular biology.
[21] J. Thornton,et al. Helix geometry in proteins. , 1988, Journal of molecular biology.
[22] J. Thornton,et al. Analysis and prediction of the different types of β-turn in proteins , 1988 .
[23] P Argos,et al. Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences , 1988, Proteins.
[24] J. Richardson,et al. Amino acid preferences for specific locations at the ends of alpha helices. , 1988, Science.
[25] P E Wright,et al. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. , 1988, Journal of molecular biology.
[26] M J Sternberg,et al. A relational database of protein structures designed for flexible enquiries about conformation. , 1989, Protein engineering.
[27] J. Thornton,et al. Beta-turns and their distortions: a proposed new nomenclature. , 1990, Protein engineering.
[28] E G Hutchinson,et al. HERA—A program to draw schematic diagrams of protein secondary structures , 1990, Proteins.