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- Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.Non-standard amino acids are derived from common amino acids by biochemical modifications. Please identify the chiral centers of given non-standard amino acids.prpc is a normal protein of our neuronal cell membrane that is sensitive to protease action (ie can be broken down by protease) true or false?
- Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. do not coy from other answers heres) This is a Fish er projecti on of D-f ructose (Fisher projecti on of L-F ructose ). Dra w L-fructose. Inaddition, draw the Haworth projection of a-D fructofuranose and b-D fructofuranose, the cyclic form ofthis monosaccharide. Draw sucrose where indicated below (Haworth projection).A protein gives, under conditions of buffer composition, pH, and temperaturethat are close to physiological conditions, a molecular weight by size exclusion measurements of 140,000 g/mol. When the same protein is studiedby SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits, and the kinds of bonding(covalent, noncovalent) existing between subunits.
- The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.The peptide bond on the C=O side of bulky hydrophobic residues is cleaved by a) Trypsin b) RNase H c) succinate dehydrogenase d) chymotrypsin e) Factor VIII ( explanation not needed) thank youBovine chymotrypsinogen has a molecular massof 25.6 kDa. Amino acid analysis shows that thisenzyme is 4.7% Gly (Mr 75.1).b. Calculate how many glycine residues are present in amolecule of bovine chymotrypsinogen
- Determine the sequence of the decapeptide given the following information below. The decapeptide was hydrolyzed and confirmed to contain these amino acids: E, F, K, M, Q, S, T x 3, W Edman degradation product of the decapeptide: T trypsin fragments: a tetrapeptide (F,K,Q,T) and a hexapeptide (E,M,S,2T,W) chymotrypsin fragments: free S, a dipeptide (F,T) and a heptapeptide (E,K,M,Q,T,T,W) CNBr treatment of the heptapeptide (E,K,M,Q,T,T,W) yielded a tetrapeptide (K,T,M,Q) and a tripeptide (E,T,W) Edman degradation product of (E,T,W): E Use one-letter abbreviations only. One amino acid per blank.Please state if the statements are true or false.1. An aplha 1,4 glycosidic linkage is considered a branching linkage in polysaccharides2. Isocitrate dehydrogenerase is classified as an isomerase2. Amino acid analysis of the a heptapeptide gave the following residues: Asp Glu Leu Lys Met Tyr Trp NH4+. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was OH H C-C-CH₂ H. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Glu, Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a tetrapeptide that had a net positive charge at pH 7 and tripeptide that had a zero net charge at pH 7. What is the amino acid sequence for this heptapeptide?