| Group 2 | Cleaving of peptide chain is done by The number of different amino acid that combine to form human protein is Taurine, non- standard amino acids, derivative of amino acids Dopamine is derivative from Group 1 Primary structure Secondary structure Tertiary structure Quaternary structure Interaction of more than more than one poly peptide chain Precipitation of proteins can be done by Domain Ammonium sulfate |Compact globular functional unit of a protein is termed as During denaturation of proteins, all of the structure is disturbed except The natural occurring proteins consist of Alcohol Proline Tyrosine L- amino acid Helix breakers is

| Group 2 | Cleaving of peptide chain is done by The number of different amino acid that combine to form human protein is Taurine, non- standard amino acids, derivative of amino acids Dopamine is derivative from Group 1 Primary structure Secondary structure Tertiary structure Quaternary structure Interaction of more than more than one poly peptide chain Precipitation of proteins can be done by Domain Ammonium sulfate |Compact globular functional unit of a protein is termed as During denaturation of proteins, all of the structure is disturbed except The natural occurring proteins consist of Alcohol Proline Tyrosine L- amino acid Helix breakers is

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

Consider the 20 standard amino acids and their structures. Choose a set of 6 amino acids that you think could theoretically be eliminated from existence and still allow proteins to fold, function, and support life with the remaining 14. Eliminating amino acids from existence would result in a need for changes to the amino acid sequence of proteins, however your choices of amino acids to eliminate should result in minimal changes to the way proteins are currently structured and function. For each amino acid that you propose to eliminate defend your choice with a 2-3 point explanation using reasoning. Your answer should be no longer than 1.5 pages in length and you should start a new paragraph for each amino acid that you select to be eliminated.
Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
Below is a schematic representation of two helices in keratin forming a coiled coil: Which amino acid residue is most likely to be found in position "a" or "d" of the pseudo repeat in? keratin? Glu Val Lys Ο Pro Trp 4
One of your patients, a six-year-old girl who suffers from Sickle cell anemia, an inherited blood disorder in which red blood cells are abnormally shaped and fragile, leading to a short supply of red blood cells. These abnormal cells can also get stuck in small vessels, which prevent blood flow, leading to fatigue, pain and other severe complications. What molecules make up each single peptide? Deoxynucleotides (dNTPs) Nucleotides (NTPs) Amino acids DNA RNA
The following structurally define nucleic acids EXCEPT They are polynucleotides connected covalent linkages. They are polyionic molecules of high molecular weight composed of a specific sequence of subunits called nucleosides. They are chainlike macromolecules that function in the storage and transfer of genetic information. Molecularly, they contain genes that encode for polypeptides and RNA molecules.
> Is the R group (CH3) on the amino acid alanine seen below, polar or non-polar? > If there were several alanines close together in a peptide chain would that bit of the chain be exposed to or folded to "hide" from water? H H N-C H-C-H 0-H
For this homework it’s a protein but I am stuck because it asks This molecule can have _____ levels of structure And then it asks What level of structure is shown in this protein marcromolecule Then asks if I add another chain to this molecule what level of structure will that be? What are the other levels of structure it can have and how are they formed
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
Hydrophobic interactions associated with protein tertiary structure involves: Acidic and basic amino acid side chains All of the above Nonpolar amino acid side chains Hydrogen bonding between polar amino acid side chains
1. what do you think a “peptide”means? 2. Proteins are extremely long, folded chains of amino acids, containing between 150-1000 amino acids linked together in a straight chain. A protein will have a long repeating chain of-N-C-C- as its backbone, with different R groups sticking out. How long could a protein be? be specific. 3. Add the C’s and H’s into their structural formulas. picture included