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Protein type number

Factor (synonym) CAS Registry Number Protein type Molecular weight, daltons Isoelectric point PPTA, %... [Pg.170]

The law of mass action controls the binding of calcium by proteins. The number and type of binding sites for calcium on the various caseins, and their association constants, have been investigated by a... [Pg.145]

As there are 19 possibilities for the introduction of proteinogenic amino acids besides the one contained in the wild-type protein, the number of possible variants of a protein obtained by introducing M substitutions over the length of the protein sequence of N amino acids is given by Eq. (11.1). [Pg.312]

Measurable loss of pyrazine concentration in the presence of soy proteins was a function of the type of protein. The number of binding sites and intrinsic binding constants on 7S, 11S, and whole soy proteins for the series of pyrazines are given in Table III. [Pg.484]

Protein Structural type Number of Number of solvent Resolution R factor a (bonds) Refinement method Reference... [Pg.361]

Natural fluorescent labeling of proteins is derived from their primary structure, i.e. mainly from the type, number and occurrence of amino acids having fluorescent properties. For native (intrinsic) fluorescence of proteins tryptophan and tyrosine are specially responsible, although some other amino acids (phenylalanine, histidine, arginine) are fluorescent, too. The fluorescence contribution of these other amino acids is, however, extremely The fluorescence of tyrosine is normally... [Pg.187]

MS channels are composed of amino acids, which are the building blocks of all proteins. The number of amino acids varies largely between different types of MS chaimels. For example, a single monomer of the bacterial chaimel MscL of E. coli is made of 136 amino acids folded in several a-helices connected by loops. A short N-terminal a-hetix of the MscL monomer is followed by two transmembrane helices TMl and TM2 and a C-terminal cytoplasmic a-helical domain (Fig. la). The TMl helix is connected to TM2 by a loop that extends into the pore region and hnes the periplasmic side of the channel. A 3-D structure of MscL obtained by X-ray crystallography has revealed that the chaimel folds as a homopentamer (Fig. la)... [Pg.966]

One popular strategy to isolate and identify the binding domain of a protein type CSP is to compare the retention and enantioselectivity behaviour of CSPs prepared with whole proteins and with isolated protein domains. Such a study has been performed by Pinkerton et al. [204) with turkey ovomucoid. Columns made from whole-turkey ovomucoid displayed chiral activity toward many racemates, whereas the fused first and second domain resolved only a selected number of aromatic weak bases. The first and second domains independently expressed no appreciable chiral recognition activity. The third domain, however, exhibited enantioselective protein binding for fused-ring aromatic weak acids, and glycosylation of this domain did not affect chiral recognition. [Pg.380]

The third type of modularity, the multi-catalytic enzymes using substrate channelling, are of particular interest for synthetic applications. Prominent members are the fatty acid synthases, the polyketide synthases and the non-ribosomal peptide synthases l42-44 . in these large proteins, a number of catalytic domains is combined with accessory domains and allows the catalysis of an entire pathway by a single polypeptide chain. Multi-catalytic enzymes frequently use a swinging arm , which is covalently attached to the intermediary product of one reaction step, and is subsequently able to present this molecule to the next catalytic domain for further... [Pg.150]


See other pages where Protein type number is mentioned: [Pg.94]    [Pg.329]    [Pg.57]    [Pg.128]    [Pg.317]    [Pg.140]    [Pg.86]    [Pg.39]    [Pg.7]    [Pg.61]    [Pg.203]    [Pg.572]    [Pg.1696]    [Pg.136]    [Pg.214]    [Pg.29]    [Pg.225]    [Pg.144]    [Pg.512]    [Pg.861]    [Pg.216]    [Pg.383]    [Pg.3911]    [Pg.175]    [Pg.289]    [Pg.253]    [Pg.86]    [Pg.216]    [Pg.159]    [Pg.289]    [Pg.95]    [Pg.248]    [Pg.145]    [Pg.19]    [Pg.118]    [Pg.76]    [Pg.261]    [Pg.263]    [Pg.287]    [Pg.156]    [Pg.82]    [Pg.30]   
See also in sourсe #XX -- [ Pg.14 ]




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Protein number

Protein, proteins number

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