In the protein whose primary sequence is provided below, which of the amino acids listed is interacting with its binding partner (such as an antibiotic)? INSTANCE RUBREDOXIN - Clostridium pasteurianum View Features in 30 PDB INSTANCEA MKKY TCTVC GYIYD PEDOD PDOG VNPGT DEKDI PODWVCEEC GVGKD EFEEVEE MKKYTCTVCGY UNIPROT ALIGN PO2S SECONDARY STRUCTURE ANGLE OUTLIER BOND OUTLIER ROTAMER OUTLIER METAL COORDINATION SNDING SITE FE CATH SCOP MOLECULE PROCESSING METAL BINDING MODIFIED RESIDUE DOMAIN STEREO OUTLIER Select one a 42 b. 10 C. 22 d. 53 e 30

In the protein whose primary sequence is provided below, which of the amino acids listed is interacting with its binding partner (such as an antibiotic)? INSTANCE RUBREDOXIN - Clostridium pasteurianum View Features in 30 PDB INSTANCEA MKKY TCTVC GYIYD PEDOD PDOG VNPGT DEKDI PODWVCEEC GVGKD EFEEVEE MKKYTCTVCGY UNIPROT ALIGN PO2S SECONDARY STRUCTURE ANGLE OUTLIER BOND OUTLIER ROTAMER OUTLIER METAL COORDINATION SNDING SITE FE CATH SCOP MOLECULE PROCESSING METAL BINDING MODIFIED RESIDUE DOMAIN STEREO OUTLIER Select one a 42 b. 10 C. 22 d. 53 e 30

Name: 3 How many beta sheets does the following protein have?INSTANCEPROCARB
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Description: 3 How many beta sheets does the following protein have?INSTANCEPROCARBOXYPEPTIDASE E- Sus scrofa View Features in 30HHSGEHFEGEKVERVNVEDENDISELHELASTROIDFWKPOSVTOIKEHSTVOFRVKAEDILAVEDFLEGNELOYEVLINNCHHRGEHEEGEKVERVNVEDENDISELHELASTROIDEWKPOSVTOIKPHSTV

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 3P: Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules,...

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Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Both hsp60-like and hsp70 molecular chaperonesshare an affinity for exposed hydrophobic patches on pro-teins, using them as indicators of incomplete folding. Whydo you suppose hydrophobic patches serve as critical sig-nals for the folding status of a protein?
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What is the overall charge on peptide AVGDWESKELLE at pH 7.0? a. -3 b. -2 c. 0 d. +1 Which of these decapeptide is the most hydrophobic? 1. ADEEEHNRQL 2. AVLKTIFYRS 3. AVLTIIFYRG 4. AVLTDNQLPK
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Apamine is a small protein toxin present in the venom of the honeybee. Ithas the sequenceCNCKAPETALCARRCQQH(a) If apamine does not react with iodoacetate (see Tools of Biochemistry5B), then how many disulfide bonds are present?(b) If trypsin cleavage gave two peptides, then where is(are) the S¬Sbond(s)?
On average, how many phosphoanhydride bonds (P;-P; bonds) are directly hydrolyzed in thecourse of synthesizing a 200 amino acid protein? Assume that you begin with the mature mRNA,ribosomal subunits, tRNAs, free amino acids, and all necessary factors.
Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?
What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weight
The following sequence is part of a globular protein. Predict the secondarystructure in this region.cRRPVVLMAACLRPVVFITYGDGGTYYHWYH c