Weak Interactions in Aqueous Systems: -Weak Interactions Are Crucial to Macromolecular Structure and Function

The noncovalent interactions we have described (hydrogen bonds and ionic, hydrophobic, and van der Waals interactions) (Table 2–5) are much weaker than covalent bonds. An input of about 350 kJ of energy is re quired to break a mole of (6X10²³) C-C single bonds, and about 410 kJ to break a mole of COH bonds, but as little as 4 kJ is sufficient to disrupt a mole of typical van der Waals interactions. Hydrophobic interactions are also much weaker than covalent bonds, although they are substantially strengthened by a highly polar sol vent (a concentrated salt solution, for example). Ionic interactions and hydrogen bonds are variable in strength, depending on the polarity of the solvent and the alignment of the hydrogen-bonded atoms, but they are always significantly weaker than covalent bonds. In aqueous solvent at 25 C, the available thermal energy can be of the same order of magnitude as the strength of these weak interactions, and the interaction between solute and solvent (water) molecules is nearly as favor able as solute-solute interactions. Consequently, hydro gen bonds and ionic, hydrophobic, and van der Waals interactions are continually formed and broken. Although these four types of interactions are individually weak relative to covalent bonds, the cumulative effect of many such interactions can be very significant. For example, the noncovalent binding of an enzyme to its substrate may involve several hydrogen bonds and one or more ionic interactions, as well as hydrophobic and van der Waals interactions. The formation of each of these weak bonds contributes to a net decrease in the free energy of the system. We can calculate the stability of a noncovalent interaction, such as that of a small molecule hydrogen-bonded to its macromolecular part ner, from the binding energy. Stability, as measured by the equilibrium constant (see below) of the binding re action, varies exponentially with binding energy. The dissociation of two biomolecules (such as an enzyme and its bound substrate) associated noncovalently through multiple weak interactions requires all these in teractions to be disrupted at the same time. Because the interactions fluctuate randomly, such simultaneous disruptions are very unlikely. The molecular stability be stowed by 5 or 20 weak interactions is therefore much greater than would be expected intuitively from a sim ple summation of small binding energies. Macromolecules such as proteins, DNA, and RNA contain so many sites of potential hydrogen bonding or ionic, van der Waals, or hydrophobic interactions that the cumulative effect of the many small binding forces can be enormous. For macromolecules, the most stable (that is, the native) structure is usually that in which weak-bonding possibilities are maximized. The folding of a single polypeptide or polynucleotide chain into its three-dimensional shape is determined by this princi ple. The binding of an antigen to a specific antibody de pends on the cumulative effects of many weak interac tions. As noted earlier, the energy released when an enzyme binds noncovalently to its substrate is the main source of the enzyme’s catalytic power. The binding of a hormone or a neurotransmitter to its cellular recep tor protein is the result of weak interactions. One con sequence of the large size of enzymes and receptors is that their extensive surfaces provide many opportunities for weak interactions. At the molecular level, the complementarity between interacting biomolecules reflects the complementarity and weak interactions between polar, charged, and hydrophobic groups on the surfaces of the molecules. When the structure of a protein such as hemoglobin (Fig. 2–9) is determined by x-ray crystallography (see

.

FIGURE 2–9 Water binding in hemoglobin. The crystal structure of hemoglobin, shown (a) with bound water molecules (red spheres) and (b) without the water molecules. These water molecules are so firmly bound to the protein that they affect the x-ray diffraction pattern as though they were fixed parts of the crystal. The gray structures with red and orange atoms are the four hemes of hemoglobin.

Box 4–4, p. XX), water molecules are often found to be bound so tightly as to be part of the crystal structure; the same is true for water in crystals of RNA or DNA. These bound water molecules, which can also be de tected in aqueous solutions by nuclear magnetic reso nance, have distinctly different properties from those of the “bulk” water of the solvent. They are, for example, not osmotically active (see below). For many proteins, tightly bound water molecules are essential to their function. In a reaction central to the process of photosyn thesis, for example, light drives protons across a biological membrane as electrons flow through a series of electron-carrying proteins (see Fig. 19–XX). One of these proteins, cytochrome f, has a chain of five bound water molecules (Fig. 2–10) that may provide a path for pro tons to move through the membrane by a process known as “proton hopping” (described below). Another such light-driven proton pump, bacteriorhodopsin, almost certainly uses a chain of precisely oriented bound water molecules in the transmembrane movement of protons (see Fig. 19–XX).

FIGURE 2–10 Water chain in cytochrome f. Water is bound in a pro ton channel of the membrane protein cytochrome f, which is part of the energy-trapping machinery of photosynthesis in chloroplasts (see Fig. 19–XX). Five water molecules are hydrogen-bonded to each other and to functional groups of the protein, which include the side chains of valine, proline, arginine, alanine, two asparagine, and two glutamine residues. The protein has a bound heme (see Fig. 5–1), its iron ion facilitating electron flow during photosynthesis. Electron flow is coupled to the movement of protons across the membrane, which probably involves “electron hopping” (see Fig. 2–14) through this chain of bound water molecules.

اخر الاخبار

اخبار العتبة العباسية المقدسة

قسم الشعائر يشارك في حملة إغاثة الشعبين الإيراني واللبناني عبر منافذ العتبة العباسية المقدسة

ضمن برنامج بيوت النعيم.. قسم الشؤون الفكرية ينظّم مجلسًا عزائيًّا في بابل

المجمَع العلمي يقيم الحفل الختامي لدورتي (زينة القرآن والإتقان القرآني) في المثنى

شعبة التوجيه الديني النسوي تنظم برنامج مفتاح البصيرة الأسبوعي

المزيد

الآخبار الصحية

الشاشات ليست مجرد ترفيه.. تأثيرات طويلة المدى على دماغ طفلك

الأسباب الرئيسية لنقص الطاقة في الجسم

الكاكاو وتأثيره على العين.. نتائج واعدة من تجارب مخبرية

طبيب يحذر: أطعمة شائعة الاستهلاك أخطر على صحتنا من التدخين

المزيد

الآخبار التكنلوجية

باحثون في "نيويورك أبوظبي" يطورون تقنيات لرصد وعلاج الأورام

جيتكس إفريقيا.. المغرب يجمع "رواد التكنولوجيا" من 103 دول

طاقم أرتميس 2 يحطم رقما قياسيا ويستعرض الجانب البعيد للقمر

"أرتيميس 2" تنطلق حول القمر وتحطم الرقم القياسي

المزيد

مواضيع ذات صلة

Ionization of Water, Weak Acids, and Weak Bases: -The pH Scale Designates the H+ and OH- Concentrations

Ionization of Water, Weak Acids, and Weak Bases: -The Ionization of Water Is Expressed by an Equilibrium Constant

Ionization of Water, Weak Acids, and Weak Bases: - Pure Water Is Slightly Ionized

Weak Interactions in Aqueous Systems: -Solutes Affect the Colligative Properties of Aqueous Solutions

Weak Interactions in Aqueous Systems: - van der Waals Interactions Are Weak Interatomic Attractions

Weak Interactions in Aqueous Systems: -Nonpolar Compounds Force Energetically Unfavorable Changes in the Structure of Water

Weak Interactions in Aqueous Systems: -Entropy Increases as Crystalline Substances Dissolve

Weak Interactions in Aqueous Systems: - Water Interacts Electrostatically with Charged Solutes

Weak Interactions in Aqueous Systems: -Water Forms Hydrogen Bonds with Polar Solutes

Weak Interactions in Aqueous Systems: - Hydrogen Bonding Gives Water Its Unusual Properties

Evolutionary Foundations: -Molecular Anatomy Reveals Evolutionary Relationships

Evolutionary Foundations: -Eukaryotic Cells Evolved from Prokaryotes in Several Stages