The primary structure of proteins results from choose the best answer) O assistance from chaperonin enzymes O the sequence of amino acid subunits that make up the protein polymer O the twisting, bending, and coiling resulting from hydrogen bonds into spirals and sheets O the folding and reshaping that results from hydrophobic interactions and the formation of disulfide bridges between cysteine amino acids in the polymer

The primary structure of proteins results from choose the best answer) O assistance from chaperonin enzymes O the sequence of amino acid subunits that make up the protein polymer O the twisting, bending, and coiling resulting from hydrogen bonds into spirals and sheets O the folding and reshaping that results from hydrophobic interactions and the formation of disulfide bridges between cysteine amino acids in the polymer

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
What is one of the determining factors in the three-dimensional structure of a protein? A.The location of alpha sheets and beta propellersB.The presence of another proteinC.The location of hydrophobic and hydrophilic amino acidsD.The presence of nucleic acids such as DNA
Which level(s) of protein structure result(s) from non-covalent interactions involving both backbone groups and side chains? (Select all that apply!) a) Primary b) Secondary c) Tertiary d) Quaternary
Indicate the level(s) of protein structure to which each of thefollowing contributes:a. amino acid sequenceb. b-pleated sheetc. hydrogen bondd. disulfide bond
Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structure
The R-group of lysine has an overall positive charge. The R-group of glutamic acid has an overall negative charge. Within the structure of a protein molecule, these two amino acids will: O attract each other O repel each other O form a disulfide bridge O form a pure covalent bond
The tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? A mutation in the genetic sequence, which ultimately causes an amino acid to change(e.g. Trp – Asn – His turns into Trp – Arg – His) Dissolving a protein in a non-polar solvent (like oil) instead of water.
Which levels of protein structure are determined by primary structure (i.e. the specific amino acid sequence beginning at the amino terminus of the polypeptide)? Mark all that apply. 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bonds
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
Which of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl end