Like a helices, ß sheets often have one side facing the surface of the protein and one side facing the interior, giving rise to an amphiphilic sheet with one hydrophobicsurface and one hydrophilic surface. From the sequences listed below, pick the one that could form a strand in an amphiphilic ß sheet.O TLNISFQMELDVO DSETKNAVFLILO VLEFMDIASVLD

Alpha-helices and beta-sheets are examples of protein secondary structures. Secondary structure…

Answered: Like a helices, B sheets often have one…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?
Please depict a noncovalent interaction important for the function of lysozyme.
Give the sequence of the LEFT (5'-end) region of this RNA strand that would participate in forming the stem of a stem-loop with this bit of RNA. DRAW this stem-loop in your scratch work! 5’-UGGUGGAUCUCUGCAACUGAUCCAUUG-3’
Which amino acid sequence will be generated? 5'-GAAUGUCUUCGUUAUUGAUGUAGAA-3'
Draw the structure of a phosphonamidite monomer suitable for SPPS of adenosine RNA Nucleosides. Circle all protecting groups and identify their canonical deprotection conditions.
show a
Pro-CHEMBIO peptide is a large peptide sequence with three disulfide bonds (indicated by the lines between cysteine residues). CHEMBIO Protease cleaves amide bonds between two basic amino acid residues to give the final peptide that is active in the body. The products of this protease reaction are: 1. Two chains that make up active CHEMBIO peptide, which contain the N- and C-terminus sections of the original Pro-CHEMBIO molecule 2. A separate inactive peptide What if instead of CHEMBIO Protease, this peptide was cleaved by trypsin? Indicate the cleavage locations on the structure below. asap
Which positions can tolerate conservative substitution?
Trypsin cleaves a polypeptide backbone at the C-terminal side of Arg or Lys residues, whereas chymotrypsin cleaves after aromatic residues. A polypeptide was treated with trypsin to generate a series of fragments of the following sequences: Gly-Gly-Ile-Arg Ser-Phe-Leu-Gly Trp-Ala-Ala-Pro-Lys Ala-Glu-Glu-Gly-Leu-Arg And the same polypeptide was treated with chymotrypsin to generate the following fragments: Leu-Gly Ala-Glu-Glu-Gly-Leu-Arg-Trp Ala-Ala-Pro-Lys-Gly-Gly-Ile-Arg-Ser-Phe Assemble the protein sequence.
w/opCulGACU GAC UC 4C According to the Genetic Code Sheet below, which of the following amino acid sequences corresponds to this MRNA strand? CỤC AAG UGC UUC PHE GLU ASP SER ALA TYR U A STOP A GU VAL U CIS U U G A STOP IG TRP ARG AC U LEU SER UG PRO ASN HIS THE GLN MET ILE ARG O a lys-leu-cys-phe O b glu-cys-pro-phe leu-lys-cys-phe O d leu-glu-leu-val U...pdf
For each altered nucleotide sequence give the type of mutation (effect at the DNA/nucleotide level; see #1 above)

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