Experimental evidence for the correlation of bond distances in peptide groups detected in ultrahigh-resolution protein structures(301 views) Esposito L, Vitagliano L, Zagari A, Mazzarella L
Protein Eng (ISSN: 0269-2139, 0269-2139print, 0269-2139linking), 2000 Dec; 13(12): 825-828.
Keywords: Amide Resonance, Crystallography, Peptide Bond, Protein Structure, Ultrahigh Resolution, Peptide Derivative, Ribonuclease A, Article, Chemical Bond, Cis Trans Isomerism, Geometry, Ligand Binding, Molecular Interaction, Priority Journal, Protein Folding, Protein Interaction, Carbon, X-Ray, Databases, Factual, Humans, Nucleic Acid Conformation, Peptide Fragments, Peptidylprolyl Isomerase, Protein Conformation, Pancreatic,
Affiliations: Centro di Studio di Biocristallografia CNR, Dipartimento di Chimica, Universita di Napoli 'Federico II', Via Mezzocannone 4, I-80134 Naples, Italy
CEINGE, Biotechnologie Avanzate, Naples, Italy
References: Allen, F.H., (1979) Acta Crystallogr., B35, pp. 2331-233
Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer E.F., Jr., Brice, M.D., Rodgers, J.R., Kennard, O., Tasumi, M., (1997) J. Mol. Biol., 112, pp. 535-542
Wiberg, K.B., Breneman, C.M., (1992) J. Am. Chem. Soc., 114, pp. 831-840
Allen, F. H., (1979) Acta Crystallogr., B35, pp. 2331-233
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer E. F., Jr., Brice, M. D., Rodgers, J. R., Kennard, O., Tasumi, M., (1997) J. Mol. Biol., 112, pp. 535-542
Cieplak, A. S., (1994) Struct. Chem., 5, pp. 85-98
Eberhardt, E. S., Loh, S. N., Hinck, A. P., Raines, R. T., (1992) J. Am. Chem. Soc., 114, pp. 5436-5437
Garman, E. F., Schneider, T. R., (1997) J. Appl. Crystallogr., 30, pp. 211-237
Genick, U. K., Soltis, S. M., Kuhn, P., Canestrelli, I. L., Getzoff, E. D., (1998) Nature, 392, pp. 206-209
Harrison, R. K., Stein, R. L., (1992) J. Am. Chem. Soc., 114, pp. 3464-3471
Jeffrey, G. A., Houk, K. N., Paddon-Row, M. N., Rondan, N. G., Mitra, J., (1985) J. Am. Chem. Soc., 107, pp. 321-326
Lamzin, V. S., Morris, R. J., Dauter, Z., Wilson, K. S., Teeter, M. M., (1999) J. Biol. Chem., 274, pp. 20753-20755
Lindley, P. F., (1999) Acta Crystallogr., D55, pp. 1654-1662
Milner-White, E. J., (1997) Protein Sci., 6, pp. 2477-2482
Sheldrick, G. M., Schneider, T. R., (1997) Methods Enzymol., 277, pp. 319-343
Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., Clardy, J., (1991) Science, 252, pp. 839-842
Walsh, M. A., Schneider, T., Sieker, L. C., Dauter, Z., Lamzin, V., Wilson, K. S., (1998) Acta Crystallogr., D54, pp. 522-546
Walter, R. L., Thiel, D. J., Barna, S. L., Tate, M. W., Wall, M. E., Eikenberry, E. F., Gruner, S. M., Ealick, S. E., (1995) Structure, 3, pp. 835-844
Wiberg, K. B., Breneman, C. M., (1992) J. Am. Chem. Soc., 114, pp. 831-840
Experimental evidence for the correlation of bond distances in peptide groups detected in ultrahigh-resolution protein structures
The structural analysis of a deamidated derivative of ribonuclease A, determined at 0.87 Angstrom resolution, reveals a highly significant negative correlation between CN and CO bond distances in peptide groups. This trend, i.e. the CO bond lengthens when the CN bond shortens, is also found in seven out of eight protein structures, determined at ultrahigh resolution (
Experimental evidence for the correlation of bond distances in peptide groups detected in ultrahigh-resolution protein structures