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of the first mutation For example, if the first mutation decreased the protein stability by removing a hydrogen-bond donor, a second mutation that changes the acceptor may result in a protein with two mutations that is just as stable as the native protein The second mutation is called a suppressor mutation

This is also a compromise (Fig 2-5) The specificity of the interaction between a protein and a small molecule or another protein is also a compromise We ve just said that charge charge and hydrogen-bond interactions don t contribute a lot to the stability of a protein because their interaction in the folded protein simply replaces their individual interaction with water The same may be said of the interaction between an enzyme and its substrate or one protein and another However, there is a huge amount of specificity to be gained in these kinds of interactions For tight binding, the protein and its ligand must be complementary in every way size, shape, charge, and hydrogen-bond donor and acceptor sites Both the protein and the ligand are solvated by water when they are separated As the two surfaces interact, water is excluded, hydrogen bonds are broken and formed, hydrophobic interactions occur, and the protein and ligand stick to each other As in protein folding and for the same reasons, the hydrophobic interaction provides much of the free energy for the association reaction, but polar groups that are removed

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10 10

Figure 2-5

The ASSOCIATION of two molecules uses the same interactions that stabilize a protein s structure: hydrophobic interactions, van der Waals interactions, hydrogen bonds, and ionic interactions To get the most out of the interaction, the two molecules must be complementary

Actual sum of values: 140

from water by the interaction must find suitable partners in the associated state Consider what happens when a nonoptimal ligand binds to the protein The binding of this modified ligand is much weaker not because it s not the right size to fit into the protein-binding site, but because the complementary group on the protein loses a favorable interaction with water that is not replaced by an equally favorable interaction with the ligand (Fig 2-6) As with the formation of secondary structure, the multiple, cooperative hydrogen bonds that can be formed between the ligand and the protein may be stronger and more favorable than hydrogen bonds that the ligand might make to water Hydrogen bonding may, in fact, make some contribution to the favorable free energy of binding of ligands to proteins

the funds and how do you effectively manage your personal investments or your client s portfolio risk in the volatile climate created by fund traders and global investing Fund managers themselves must learn to improve risk management in order to maintain positive returns in volatile markets or the assets may travel to the fund next door Let s look at the major groups of market participants and how they are constructed and what their individual trading goals are

Now that you understand the basis for the interactions between functional groups in water, you also understand the basis for most interactions: DNA DNA, DNA RNA, DNA protein, RNA protein, protein protein, protein ligand, enzyme substrate (Get the picture ), antibody antigen, protein chromatography column it s all the same stuff

10 10 10 10 10 20 10 10 10

Figure 2-6

SPECIFICITY in the association of two proteins or a protein and a small molecule results from the requirement that the two interacting molecules must be complementary complementary in charge, hydrogen bonding, and hydrophobic patches as well as shape If any of the possible interactions are not satisfied, the strength of the interaction suffers

Returned sum of values: 120

General Membrane Function Membrane Composition Phospholipid Bilayer Membrane Structure Posttranslational Modification Membrane Fluidity Diffusion in Membranes Movement of Ions and Molecules Across Membranes Transport Across Membranes The Nernst Equation

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