Structural biochemistry structure determination

Miao M, Cirulis JT, Lee S et al (2005) Structural determinants of cross- linking and hydrophobic domains for self-assembly of elastin-like polypeptides. Biochemistry 44 14367-14375... 

Grams F, Crimmin M, Hinnes L, Huxley P, Pieper M, Tschesche H, Bode W. Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry 1995 34 14012-14020. 

Cyclic phosphoric esters, especially adenosine 3, 5 -monophosphate (cAMP) and to a lesser extent guanosine 3, 5 -monophosphate (cGMP), are ubiquitous intracellular secondary messenger substances which play an important role in biochemistry. X-ray structures and NMR data have been reported and their conformations are shown in Figure 2 (see also an X-ray structural determination of the sodium salt (82JA3398)). 

In April 1992, the structure determination paper appeared in Biochemistry. This paper contains a full description of the experimental work, and a complete analysis of the structure. The following is from the 4/92 paper, "Abstract" section ... 

Otter, A., Scott, P. G., and Kotovych, G. (1988). Type-I collagen a-lchain C-telopep-tide—Solution structure determined by 600 MHz proton NMR spectroscopy and implications for its role in collagen fibrillogenesis. Biochemistry 27, 3560-3567. 

T. Kurth, D. Ullmann, H.-D. Jakubke, and L. Hedstrom, Converting trypsin to chymotrypsin Structural determinants of SI specificity, Biochemistry 1997, 36, 10098-10104. 

Cytochrome c (cyt. c) has become a major protein for testing new approaches and techniques in protein science.1 This is partly due to the venerable position that cytochrome c holds in the field of biochemistry since it was isolated and characterized more than 70 years ago. Cyt. c was one of the first proteins to be sequenced,2 and to have its X-ray structure determined in 1967.3 Cyt. c also has the advantage of stability and a spectroscopically distinct heme group. More than 23,000 articles mentioning cyt. c were published between 1945-2002 (ISI Web of Science). Here, we describe an approach to tetraphenylporphyrin-based protein surface receptors and the characterization of their interactions with the principal target cyt. c. 

Laing, L. G., and Hall, K. B. (1996). A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data. Biochemistry 35, 13586-13594. 

Mass spectrometry has provided a wealth of information on chemical structural determination, identification, and a trace level chemical analysis. It has many applications in the biochemistry, pharmaceutical, and clinical diagnostic research field. 

During the tow past decades die amount of information gathered in the area of the organic chemistry has increased tremendously. To see this vast amount of knowledge has been reflected in elementary organic chemistiy courses, one need only look at the organic chemistry texts whish have been appeared on the market in the last five years. Most of the renew texts emphasize a core of reactions, mechanisms and structure determinations via spectral properties. These subjects are then supplemented with special topics such as biochemistry, polymer chemistry and natural products. 

Li T, Quillin TL, Phillips GN, Olson JS. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry 1994 33 1433-1446. 

Mass spectrometry is one of the major techniques in the interdisciplinary field of proteomics. It provides a rapid, sensitive and reliable means of protein identification and structural determination, allowing for development in this newly baptised but yet classical field of biochemistry and biomedicine. The use of electrospray ionisation in conjunction with a tandem mass spectrometer (MS/MS) provides essential amino acid sequence information from the m/z values of the so-called b andy ions formed from cleavage of the amide bond of a protonated peptide. This reaction requires proton catalysis, and the mechanism is of interest in the present context, since it is closely related to the processes occurring in other protonated carboxylic acid derivatives. 

A few studies of small groups of compounds, such as porphyrins and terpenoids are described here. A brief survey of labeled Mannich bases, particularly useful as tracers in biochemistry or as tools for structure determination, is also given. 

NMR is not a technique for everyday use in the biochemistry laboratory. The equipment needed for protein structure determination is expensive, and detailed expertise is needed to evaluate and interpret the results. For these reasons NMR as a tool in the study of biomolecular structure and function is confined to a limited number of specialist centres. 

Howell SC, Mesleh MF, Opella SJ. NMR structure determination of a membrane protein with two transmembrane helices in micelles MerF of the bacterial mercury detoxification system. Biochemistry 2005 44 5196-5206. 

Jia, X., Reisman, J. M., Hsu, V. L., Geiduschek, E. P., Parello, J. Kearns, D. R. (1994). Proton and nitrogen NMR sequence-specific assignments and secondary structure determination of the Bacillus subtilis SPOl-encoded transcription factor 1. Biochemistry 33, 8842-8852. 

K. Wakamatsu, D. Kohda, H. Hatanaka, Structure-activity relationships of mu-conotoxin GIIIA structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealbig calculations. Biochemistry, 31... 

Brandsch, M., Knutter, 1.1., Thunecke, F., Hartrodt, B., Born, 1.1., Borner, V., Hirche, F., Fischer, G. et al. (1999) Decisive structural determinants for the interaction of proline derivatives with the intestinal H+/peptide symporter. European Journal of Biochemistry, 266, 502-508. 

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