Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Protein disorders

To obtain statistically significant comparisons of ordered and disordered sequences, much larger datasets were needed. To this end, disordered regions of proteins or wholly disordered proteins were identified by literature searches to find examples with structural characterizations that employed one or more of the following methods (1) X-ray crystallography, where absence of coordinates indicates a region of disorder (2) nuclear magnetic resonance (NMR), where several different features of the NMR spectra have been used to identify disorder and (3) circular dichroism (CD) spectroscopy, where whole-protein disorder is identified by a random coil-type CD spectrum. [Pg.50]

The results described in Section I suggest that amino acid sequence codes for intrinsic protein disorder. In this circumstance, constructing a predictor of order and disorder would be useful as a means to extend and generalize from the current experimental results. [Pg.60]

The rich proteins from shrimp and crab are a positive notion nowadays for the supplementing of high ranked nutrition for many of the patients of nutrition depletion. The collagen and other protein disorders can be overcome by the intake of these crustaceans regularly. However, the financial limitations and the inadequacy of fishing profound disturbances due to the human population and pollution many of the developing nations are underutilize these animals. In addition, chitin and its derivatives are vastly known for their biomedical importance however, the utilization of the crustacean foods is restricted mostly to Asian countries, and many of the developed, developing, and underdeveloped countries are henceforth advised well for the proper implementation of these medicinally valuable resources. [Pg.7]

A-6) Protein disorders form a vast category that includes not only the numerous enzyme defects in Biochemistry land but many other defects of proteins that are not enzymes. These are far too numerous to describe in detail, but include diseases of transport proteins (e.g., the hemoglobinopathies, hypoalbuminemia) disorders of the immune system (abnormal antibodies in autoimmune and other immune disorders—fig. 10.1) blood dotting disturbances (e.g., the hemophilias, excess thrombosis) abnormalities of cell membranes (e.g., defective cell surface receptors) and abnormalities of those hormones that are proteins. Many of these disorders are primary defects that stem from gene mutation. Others may be acquired. [Pg.59]

Braken C, Iakoucheva LM, Romero PR, Dunker AK (2004) Combining prediction, computation and experiment for the characterization of protein disorder. Curr Opin Struct Biol 14 570-576... [Pg.160]

It wiU be evident from the section on processes of digestion and absorption that the pancreas plays a central role in the absorptive process for carbohydrates, fats, and proteins. Disorders of the exocrine pancreas are therefore frequently associated with GI symptoms of malabsorption or diarrhea. In this section, pediatric and adult exocrine pancreatic disorders are briefly discussed and tests for assessing exocrine pancreatic function are described. Information on exocrine pancreatic tumors can be found in the later section on GI regulatory peptides. Recent textbooks on gastroenterology or medicine have more detail on the clinical aspects of exocrine pancreatic disorders. [Pg.1867]

Linding, R., L. J. Jensen, F. Diella, P. Bork, T. J. Gibson, and R. B. Russell. 2003. Protein disorder prediction Implications for structural genomics. Structure 11 1453-9. [Pg.77]

Deng, X., Eickholt, J., Cheng, J. (2012) A comprehensive overview of computationeil protein disorder prediction methods. Mol Biosyst, 8(1), 114-121. [Pg.318]

Schlessinger, A., Schaefer, C., Vicedo, E., et al. (2011) Protein disorder—a breakthrough invention of evolution Curr Opin Struct Biol, 21 (3), 412-418. [Pg.319]

R472 R. Schneider, J.-r. Huang, M. Yao, G. Communie, V. Ozenne, L. Mollica, L. Salmon, J. M. Ringkjobing and M. Blackledge, Towards a Robust Description of Intrinsic Protein Disorder Using Nuclear Magnetic Resonance Spectroscopy , Mol. BioSyst., [online computer file], 2012, 8, 58. [Pg.53]

Second derivative FT-IR spectra of Mb-DMPC films (Fig. 8b) at pH 6 and 7 are similar to those of Mb alone. The band at 1742 cm is from DMPC ester carbonyl stretch. As pH decreases from 7 to 4, the a-helix band for Mb-DMPC films at 1657-1659 cm decreases and is accompanied by a new band at 1630 cm indicating increased protein disorder. This latter peak is clearly evident at pH 5, and is stronger at pH 4 (Fig. 8b). The new band suggests unfolding of helices at low pH compared to the native Mb structure. Second derivative spectra for Mb-DDAB also showed a band at 1630 cm at pH 4, but not at pH 7.5, confirming increased extended chain features as pH decreased. [Pg.183]

Z. Dosztanyi and P. Tompa, Prediction of Protein Disorder , in Methods in Molecular Biology (Totowa, NJ, United States), eds. B. Kobe, M. Guss and Th. Huber, Humana Press Inc, 2008, vol. 426, Structural Proteomics, p. 103. [Pg.30]

R 71 J.E. Landbury and M.A. Williams, The Extended Interface Measuring Non-Local Effects in Biomolecular Interactions , p. 562 R 72 C. Bracken, L.M. lakoucheva, P.R. Romero and A.K. Dunker, Combining Prediction, Computation and Experiment for the Characterization of Protein Disorder , p. 570... [Pg.31]


See other pages where Protein disorders is mentioned: [Pg.273]    [Pg.228]    [Pg.48]    [Pg.65]    [Pg.68]    [Pg.69]    [Pg.229]    [Pg.564]    [Pg.318]    [Pg.319]    [Pg.234]    [Pg.689]    [Pg.955]    [Pg.314]    [Pg.329]    [Pg.330]    [Pg.915]   
See also in sourсe #XX -- [ Pg.92 ]




SEARCH



Amino acid sequence ordered/disordered proteins

Circular dichroism disordered proteins

Disordered aggregates, protein crystallization

Disordered proteins

Disordered proteins

Disordered proteins PONDRs

Disordered proteins characterization methods

Disordered proteins comparisons

Disordered proteins disorder prediction

Disordered proteins hydrogen exchange kinetics

Disordered proteins overview

Disordered proteins sequence attributes

Disordered proteins, intrinsically

Disordered regions, of protein

Evolution, disordered proteins

Folding of an Intrinsically Disordered Protein Upon Binding to a Target

Intrinsically Disordered Region of Proteins

Intrinsically disordered proteins detection

Intrinsically disordered proteins residual structure

Kinetics of Hydrogen Exchange in Disordered Proteins

Millisecond disordered protein studies

Natively disordered proteins, models

Protein crystal disorder

Protein digestion disorders

Protein folding disorders

Protein structure disordered structures

Proteins patients with metabolic disorders

Residual Structure in Intrinsically Disordered Proteins

© 2024 chempedia.info