Question

1. which functionaal groups are present on the backbone of every amino acid? 2. is polypeptide...

1. which functionaal groups are present on the backbone of every amino acid?


2. is polypeptide is a protein?


3. at the secondary level of protein structure what types of bonds occur between components of the polypeptide backbone ?

Homework Answers

Answer #1

Ans.1.

All amino acids have the same backbone structure, with an amino group ,a carboxyl group, an α-hydrogen, and a variety of functional groups (R) all attached to the α -carbon.

Ans.2.

no, polypeptide is not a protein but Protein is a polypeptide.

Polypeptide refers to a polymer linked by peptide bonds.So a polypeptide has amino acids as the monomer unit. All proteins are polypeptides. But all polypeptides are not because A polypeptide is a single linear chain of many amino acids (any length), held together by amide bonds.

A protein consists of one or more polypeptides (more than about 50 amino acids long). An oligopeptide consists of only a few amino acids (between two and twenty).

Ans 3

Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone.

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
1.Amino acid breakdown, backbone of amino acid could submit to which intermediates in TCA cycle (answer...
1.Amino acid breakdown, backbone of amino acid could submit to which intermediates in TCA cycle (answer all) 2.What is the type of shuttle that used to transport fatty acid between organelle ? 3.Proteosomal degradation uses …. ....….. to mark target protein prior committed to degradation. 4.Glycogenin is a protein primer used to build glycogen produce from which amino acid?  
Which of the following statements is FALSE? A)Both -helices and -sheets have R groups that are...
Which of the following statements is FALSE? A)Both -helices and -sheets have R groups that are oriented away from the core of the structure. B)Both -helices and -sheets are stabilized by hydrogen bonds between groups in the polypeptide backbone. C)Both -helices and -sheets have conformations that minimize steric strain in the polypeptide backbone. D)Both -helices and -sheets form only from adjacent (sequential) amino acid residues in the polypeptide.
You wish to determine the sequence of a polypeptide that has the following amino acid composition....
You wish to determine the sequence of a polypeptide that has the following amino acid composition. 1 Ala 4 Arg 2 Asn 3 Asp 4 Cys 3 Gly 1 Gln 4 Glu1 His 1 Lys 1 Met 1 Phe 2 Pro 4 Ser 2 Tyr 1 Trp What is the maximum number of peptides you can expect if you cleave the polypeptide with cyanogen bromide ? What is the maximum number of peptides you can expect if you do a...
1. For protein secondary structure, which of the following is incorrect? A. Secondary structure consists of...
1. For protein secondary structure, which of the following is incorrect? A. Secondary structure consists of α-helices and β-pleated sheets B. The interactions between C=O and N-H groups are hydrogen bonding interactions C. Secondary structure is created by bonding between C=O and N-H groups in the peptide backbone D. A protein can have either α-helices of β-pleated sheets, but never both 2. With regard to protein folding and denaturation, which one is incorrect? When egg white solidifies during heating, this...
A. Separate cleavage reactions of polypeptide by CNBrand chymotrypsin yield fragments with the following amino acid...
A. Separate cleavage reactions of polypeptide by CNBrand chymotrypsin yield fragments with the following amino acid sequences. What is the sequence of the intact polypeptide? CNBr treatment ​1. Arg-Ala-Tyr-Gly-Asn ​2. Leu-Phe-Met ​3.Asp-Met Chymotrypsin ​1. Met-Arg-Ala-Tyr ​2. Asp-Met-Leu-Phe ​3. Gly-Asn B. The pKa of the carboxylic acid is around 3, and the pKa of the protonated amino group is around 10. Which of the structures below best represents an amino acid at neutral pH (i.e.,pH = 7)? Select one: a. +H3NCHRCOOH...
Match the following levels of protein structure with the description. 1. Interactions of multiple peptides coded...
Match the following levels of protein structure with the description. 1. Interactions of multiple peptides coded by the same of different genes to form a single functional unit 2. Functional domains dictated by unique interactions between amino acid R groups in the peptide chain 3. Interaction of multiple proteins with distinct functions dictate by unique non-covalent interactions between R groups of each factor in the complex. 4. Level of structure formed during ribosomal synthesis, ultimately contributing to the formation of...
Describe how the structure of a protein forms for each of the following levels of protein...
Describe how the structure of a protein forms for each of the following levels of protein formation. Include the type(s) of bonds formed and specifically what part of the polypeptide/amino acids these bonds form between. 1. Secondary 2. Tertiary
Carboxypeptidase, which sequentially removes carboxy-terminal amino acid residues from its peptide substrates, is a single polypeptide...
Carboxypeptidase, which sequentially removes carboxy-terminal amino acid residues from its peptide substrates, is a single polypeptide of 307 amino acids. The two essential catalytic groups in the active site are furnished by Arg145 and Glu270. (a) If the carboxypeptidase chain were a perfect α-helix, how far apart (in Å) would Arg145 and Glu270 be? Hint: See Fig 4-4a. (b) Explain how the two amino acid residues can catalyze a reaction occurring in the space of a few angstroms.
Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about...
Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. Based on the possibility of 2.7×1092 conformations, estimate the conformational entropy change on folding a mole of this protein into a native structure with only one conformation.
Which of the following statements is true concerning the tertiary (3°) structure of proteins? Beta sheet...
Which of the following statements is true concerning the tertiary (3°) structure of proteins? Beta sheet is an example of this type of structure Often held together by disulfide bonds Only held together by peptide bonds Refers to the amino acid sequence of a protein Refers to the association of two or more polypeptide chains together