Peptide models XXIX. cis-trans Isomerism of peptide bonds: ab initio study on small peptide model compound; the 3D-Ramachandran map of formylglycinamide
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Imre G. Csizmadia | András Perczel | Ricardo D. Enriz | Ödön Farkas | Héctor A. Baldoni | R. Enriz | H. Baldoni | A. Perczel | I. Csizmadia | Ö. Farkas | Salvatore J. Salpietro | Graciela N. Zamarbide | E. A. Jáuregui | E. Jáuregui | G. Zamarbide | G. N. Zamarbide
[1] F. Richards,et al. Folding kinetics of phage T4 thioredoxin. , 1990, Biochemistry.
[2] F. Naider,et al. Proline-dependent structural and biological properties of peptides and proteins. , 1993, Critical reviews in biochemistry and molecular biology.
[3] P. Andrews. Cis–Trans isomerism of the peptide bond , 1971, Biopolymers.
[4] E. Blout,et al. Nuclear magnetic resonance evidence for cis-peptide bonds in proline oligomers. , 1970, Journal of the American Chemical Society.
[5] D. Pérahia,et al. Molecular orbital calculations on the conformation of polypeptides and proteins. IV. The conformation of the prolyl and hydroxyprolyl residues. , 1970, Journal of theoretical biology.
[6] F. Schmid,et al. Role of two proline-containing turns in the folding of porcine ribonuclease. , 1990, Journal of molecular biology.
[7] T. Kiefhaber,et al. Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. , 1992, Journal of molecular biology.
[8] Richard S. Rosenstein,et al. Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. , 1992, Biochemistry.
[9] N. Richards,et al. Probing the role of proline as a recognition element in peptide antigens. , 1990, Biochemical pharmacology.
[10] Roland L. Dunbrack,et al. Cis-Trans Imide Isomerization of the Proline Dipeptide , 1994 .
[11] C. Deber,et al. Proline residues in transmembrane helices: structural or dynamic role? , 1991, Biochemistry.
[12] C. Levene. Book Review: Treatise on Collagen , 1969 .
[13] 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.
[14] Kenneth B. Wiberg,et al. Barriers to rotation adjacent to double bonds. 3. The carbon-oxygen barrier in formic acid, methyl formate, acetic acid, and methyl acetate. The origin of ester and amide resonance , 1987 .
[15] E. Stellwagen,et al. A kinetic study of the folding of staphylococcal nuclease using size-exclusion chromatography. , 1992, Biochemistry.
[16] C. R. Fourtner,et al. Identification of a proline residue as a transduction element involved in voltage gating of gap junctions , 1993, Nature.
[17] J. Wess,et al. Functional role of proline and tryptophan residues highly conserved among G protein‐coupled receptors studied by mutational analysis of the m3 muscarinic receptor. , 1993, The EMBO journal.
[18] M. Robb,et al. Non-empirical LCAO-MO-SCF-CI calculations on organic molecules with Gaussian type functions , 1966 .
[19] T. Kiefhaber,et al. Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1. , 1992, Journal of molecular biology.
[20] S. Lemaire,et al. Total synthesis of camel beta-melanotropin by the solid-phase method. , 1975, Biochemistry.
[21] J. Stewart,et al. Probing the role of proline in peptide hormones. NMR studies of bradykinin and related peptides. , 1990, Biochemical pharmacology.
[22] C. Deber,et al. Hypothesis about the function of membrane-buried proline residues in transport proteins. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[23] L. Nilsson,et al. Structural fluctuations between two conformational states of a transmembrane helical peptide are related to its channel-forming properties in planar lipid membranes. , 1993, European journal of biochemistry.
[24] K. Wüthrich,et al. Nmr studies of the rates of proline cis–trans isomerization in oligopeptides , 1981 .
[25] A. Yaron. The role of proline in the proteolytic regulation of biologically active peptides , 1987, Biopolymers.