Spectroscopic evidence that monoclonal antibodies recognize the dominant conformation of medium-sized synthetic peptides.

[1]  G. Fasman,et al.  The evaluation of type I and type II beta-turn mixtures. Circular dichroism, NMR and molecular dynamics studies. , 2009, International journal of peptide and protein research.

[2]  M. Shoham.  Crystal structure of an anticholera toxin peptide complex at 2.3 A. , 1993, Journal of molecular biology.

[3]  G. Fasman,et al.  Ca2+‐induced conformational transitions of phosphorylated peptides , 1993, Biopolymers.

[4]  Virginia M. Y. Lee,et al.  Recognition of the minimal epitope of monoclonal antibody Tau‐1 depends upon the presence of a phosphate group but not its location , 1993, Journal of neuroscience research.

[5]  S. Lolov,et al.  Conformation-sensitive immunoassay: optimisation, validation and evaluation. , 1993, JIM - Journal of Immunological Methods.

[6]  H. Mantsch,et al.  Human and rodent Alzheimer beta-amyloid peptides acquire distinct conformations in membrane-mimicking solvents. , 1993, European journal of biochemistry.

[7]  I. Wilson,et al.  Structural evidence for induced fit as a mechanism for antibody-antigen recognition. , 1994, Science.

[8]  D. Speicher,et al.  Microsequence analysis of electroblotted proteins. II. Comparison of sequence performance on different types of PVDF membranes. , 1992, Analytical biochemistry.

[9]  L. Otvos,et al.  A serine-->proline change in the Alzheimer's disease-associated epitope Tau 2 results in altered secondary structure, but phosphorylation overcomes the conformational gap. , 1992, Biochemical and biophysical research communications.

[10]  V. Lee,et al.  Immunological and conformational characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease , 1992 .

[11]  M. Levitt,et al.  Induced peptide conformations in different antibody complexes: molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints. , 1992, Biochemistry.

[12]  F. Blanco,et al.  Periodic properties of proton conformational shifts in isolated protein helices. An experimental study. , 1992, European journal of biochemistry.

[13]  H. Kamaya,et al.  Biphasic effects of alcohols on the phase transition of poly(L-lysine) between alpha-helix and beta-sheet conformations. , 1992, Biochemistry.

[14]  G. Fasman,et al.  Conformational and functional properties of peptides covering the intersubunit region of influenza virus hemagglutinin. , 1992, European journal of biochemistry.

[15]  Y. Paterson.  Mapping antibody binding sites on protein antigens , 1992, Nature.

[16]  G. Fasman,et al.  Metal ion-induced conformational changes of phosphorylated fragments of human neurofilament (NF-M) protein. , 1992, Journal of molecular biology.

[17]  V. Lee,et al.  Reversible β-pleated sheet formation of a phosphorylated synthetic τ peptide , 1992 .

[18]  H. Mantsch,et al.  Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. , 1992, Biochimica et biophysica acta.

[19]  P. Davies,et al.  Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. , 1992, The Journal of biological chemistry.

[20]  C. Dobson,et al.  Antigen mobility in the combining site of an anti-peptide antibody. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[21]  F. Blanco,et al.  Tendamistat (12–26) fragment , 1991 .

[22]  J H Welsh,et al.  Synthesis, conformational properties, and antibody recognition of peptides containing beta-turn mimetics based on alpha-alkylproline derivatives. , 1991, Journal of medicinal chemistry.

[23]  J. Wands,et al.  Stability of monoclonal antibody-defined epitopes. , 1991, Journal of immunological methods.

[24]  R L Stanfield,et al.  Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 A. , 1992, Science.

[25]  M. Kirschner,et al.  Phosphorylation of microtubule‐associated protein tau: identification of the site for Ca2(+)‐calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles. , 1990, The EMBO journal.

[26]  L. Otvos,et al.  Reversed-phase high-performance liquid chromatographic separation of synthetic phosphopeptide isomers. , 1990, Journal of chromatography.

[27]  J. Tuls,et al.  Peptide alpha-helicity in aqueous trifluoroethanol: correlations with predicted alpha-helicity and the secondary structure of the corresponding regions of bovine growth hormone. , 1990, Biochemistry.

[28]  W. Pfund,et al.  The conformation-sensitive immunoassay: a membrane based ELISA system for identifying antibodies sensitive to alterations of protein conformation. , 1990, Molecular immunology.

[29]  J. Tam,et al.  Multiple antigen peptide. A novel approach to increase detection sensitivity of synthetic peptides in solid-phase immunoassays. , 1989, Journal of immunological methods.

[30]  J. Claverie,et al.  Conformational analysis of t immunogenic peptides by circular dichroism spectroscopy , 1989, European journal of immunology.

[31]  L. Otvos,et al.  Induction of rabies virus-specific T-helper cells by synthetic peptides that carry dominant T-helper cell epitopes of the viral ribonucleoprotein , 1989, Journal of virology.

[32]  L. Otvos,et al.  Breakage in alpha-helix: a recognition site for anti-rabies virus ribonucleoprotein antibody. , 1989, Peptide research.

[33]  G. Fasman,et al.  Phosphorylation loops in synthetic peptides of the human neurofilament protein middle-sized subunit , 1988, Journal of protein chemistry.

[34]  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.

[35]  P E Wright,et al.  Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. , 1988, Journal of molecular biology.

[36]  L. Otvos,et al.  Identification of the major multiphosphorylation site in mammalian neurofilaments. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[37]  M T Hearn,et al.  High-performance liquid chromatography of amino acids, peptides and proteins. LXXXV. Evaluation of the use of hydrophobicity coefficients for the prediction of peptide elution profiles. , 1988, Journal of chromatography.

[38]  R. Schwyzer,et al.  Membrane structure of bombesin studied by infrared spectroscopy. Prediction of membrane interactions of gastrin-releasing peptide, neuromedin B, and neuromedin C. , 1987, Biochemistry.

[39]  H. M. Geysen,et al.  Strategies for epitope analysis using peptide synthesis. , 1987, Journal of immunological methods.

[40]  M. Hearn,et al.  High-performance liquid chromatography of amino acids, peprtides and proteins , 1987 .

[41]  J. Goding,et al.  Monoclonal Antibodies: Principles and Practice , 1996 .

[42]  R. Lewis,et al.  Role of conformational changes in the elution of proteins from reversed-phase HPLC columns. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[43]  R. Jemmerson,et al.  Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes. , 1986, Science.

[44]  N. Kallenbach,et al.  Stabilization of the ribonuclease S‐peptide α‐helix by trifluoroethanol , 1986 .

[45]  A. Frankfurter,et al.  The distribution of tau in the mammalian central nervous system , 1985, The Journal of cell biology.

[46]  G. Fasman,et al.  Studies on proline‐containing tetrapeptide models of β‐turns , 1985 .

[47]  R. Woody.  Chapter 2 – Circular Dichroism of Peptides , 1985 .

[48]  R. Lerner.  Antibodies of predetermined specificity in biology and medicine. , 1984, Advances in immunology.

[49]  L. Bernini,et al.  Development of a screening system for detection of somatic mutations. II. The use of peptides and insoluble protein fragments in a non-competitive solid-phase enzyme immunoassay. , 1983, JIM - Journal of Immunological Methods.

[50]  J. Berzofsky,et al.  Topographic antigenic determinants recognized by monoclonal antibodies to sperm whale myoglobin. , 1982, The Journal of biological chemistry.

[51]  E. Blout,et al.  Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins. , 1981, Biochemistry.

[52]  G. Allen,et al.  Sequencing of proteins and peptides , 1981 .

[53]  K. Kopple,et al.  Reverse Turns in Peptides and Protein , 1980 .

[54]  M. Atassi,et al.  Antigenic structure of myoglobin: the complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins. , 1975, Immunochemistry.

[55]  R. Arnon,et al.  Immunochemistry of Enzymes , 1973 .

[56]  L. Masotti,et al.  Circular dichroism of biological membranes. I. Mitochondria and red blood cell ghosts. , 1971, Biochimica et biophysica acta.

[57]  C B Anfinsen,et al.  Antibodies reactive with native lysozyme elicited by a completely synthetic antigen. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[58]  E. Patrone,et al.  The effect of aliphatic alcohols on the helix-coil transition of poly-L-ornithine and poly-L-glutamic acid. , 1970, The Journal of biological chemistry.

[59]  G. Fasman,et al.  Computed circular dichroism spectra for the evaluation of protein conformation. , 1969, Biochemistry.