Electrostatic interactions among amino acid residues on proteins may be damped out by high concentrations of: water. organic solvents. salts. heat.
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Electrostatic interactions among amino acid residues on proteins may be damped out by high concentrations of: water. organic solvents. salts. heat.
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- Hydrogen bonds and hydrophobic interactions play important roles in stabilizing and organizing biological macromolecules. Describe how hydrogen bonds and hydrophobic interactions affect the form and function of proteins.Please describe the non-covalent interactions that exist in protein solution (proteins were dissolved in water) and describe their characteristics.Affinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the above
- Calculate the approximate molecular weight of a protein composed of 587 amino acid residues in a single polypeptide chain. approximate weight: in kDaWhich of the following is true about a peptide bond: Electron delocalization occurs between the a-amino group of one residue and the a-carbon of the subsequent residue The peptide bond is freely rotatable along its bond axis The peptide bond contains 5 co-planar atoms Dehydration to link two residues occurs due to thermodynamic coupling to high-energy phosphate hydrolysis None of the answers are correctWhich of the following statements is TRUE for nonpolar amino acid residues of polypeptides or proteins in an aqueous solution? None of the above They are hydrophilic and found buried within proteins They are hydrophilic and found on protein surfaces They are hydrophobic and found on protein surfaces They are hydrophobic and found buried within proteins
- A protein’s shape depends partly on electrical attractions between charged or polarized groups in various regions of the protein. True or false?Label: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.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
- Explain the role of hydrophobic exclusion during protein folding (tertiary structure); what type of aminoacids would you find towards the center of the protein? Charged? Polar? Non-polarDrag each of the following items into the corresponding boxes to indicate the protein structural level that is predominantly affected by the chemical interactions listed. Some items may be placed in more than one box. Reset Help Hydrogen bonds between polar groups in amino acid side chains Hydrophobic interactions between amino acid side chains lonic bonds between positively- charged and negatively-charged amino acid side chains Peptide bonds Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone Disulfide bonds Primary structure Seconday structure Tertiary structure Quaternary structureThe use of salt bridges or hydrophobic interactions (or pockets) to stabilize interactions between more distant amino acids within a single polypeptide, is a demonstration of protein QUATERNARY structure. True False