Principles of Biology
Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Chapter 3, Problem 7TY
Summary Introduction

Introduction:

Amphipathic molecules are those having both hydrophilic and hydrophobic parts. Hydrophobic as name represent hydro mean water phobic mean hate which mean water hating. Example oils and fats. Hydrophilic mean water loving which attract by water.

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Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?
In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains.  Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.
Bradykinin, a peptide that helps to regulate blood pressure, has the primary structure Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg.(a) Draw the complete structural formula of bradykinin.(b) Bradykinin has a very kinked secondary structure.Why?
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