Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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In hemoglobin (above), which level of protein organization includes the peptide bonds, hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waal forces holding this protein together?
- the primary structure
- the secondary structure
- the tertiary structure
- the quaternary structure
- all of the above
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- Lable out the main difference of Primary, secondary, tertiary, and quatrenary protein structure in biochemistryarrow_forwardWhich of the following factor(s) may contribute to the stability of folded protein structures? Disulfide bonds. Hydrophobic effect. Electrostatic interactions. Hydrogen bonds. All of the above.arrow_forward> 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-Harrow_forward
- Can you help me to explain to me?arrow_forwardWhere is hydrogen bonding observed in proteins? Between one part of the protein backbone and another part of the protein backbone Between R groups Between the protein backbone and an R group All of the abovearrow_forwardWhen one categorizes a protein's structural classification, they sort different proteins primarily based upon by their_ O secondary structure content and arrangement. amino acid sequence. evolutionary relationships. function. subunit content and arrangement.arrow_forward
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