PDF NOTES ACADEMY LIFE SCIENCESPDF Notes Academy UNIT -1 MOLECULES AND THEIR INTERACTION RELEVANT. TO BIOLOGY Protein structure g Interactive diagram of protein structure, using PCNA as an example. (PDB: 1AXC) Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers — specifically polypeptides — formed from sequences of amino Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy acids, the monomers of the polymer. A single amino acid monomer may also be called a residue indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein." To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, cryo electron microscopy (cryo-EM) and dual polarisation interferometry to determine the structure of proteins. Protein structures range in size from tens to several thousand amino acids.”! By physical size, proteins are classified as nanoparticles, between 1-100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament. A protein usually undergoes reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different conformations, and transitions between them are called conformational changes. in Contents 1Levels of protein structure Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy 1.1Primary structure 1.2Secondary structure 1.3Tertiary structure © 1.4Quaternary structure 2Domains, motifs, and folds in protein structure © 2.1Structural domain © 2.2Structural and sequence motifs 2.3Supersecondary structure © 2.4Protein fold 3Protein dynamics and conformational ensembles 4Protein folding 5Protein stability 6Protein structure determination 7Protein structure databases 8Structural classifications of proteins 9Computational prediction of protein structure 10See also 11References 12Further reading Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy + 13External links Levels of protein structure[edit] There are four distinct levels of protein structure. Four levels of protein structure Primary structure[edit] Main article: Protein primary structure The primary structure of a protein refers to the sequence of amino acids in the polypeptide chain. The primary structure is held together by peptide bonds that are made during the process of protein biosynthesis. The two ends of the polypeptide chain are referred to as the carboxyl terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each extremity. Counting of residues always starts at the N- terminal end (NH2-group), which is the end where the amino group is not involved in a peptide bond. The primary structure of a protein is determined by the gene corresponding to the protein. A Call/Whatsapp- 9166830064 PDE Notes Academy Page 5PDF Notes Academy specific sequence of nucleotides in DNA is transcribed into mRNA, which is read by the ribosome in a process called translation. The sequence of amino acids in insulin was discovered by Frederick Sanger, establishing that proteins have defining amino acid sequences./ll4l The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a protein can be determined by methods such as Edman degradation or tandem mass spectrometry. Often, however, it is read directly from the sequence of the gene using the genetic code. It is strictly recommended to use the words "amino acid residues" when discussing proteins because when a peptide bond is formed, a water molecule is lost, and therefore proteins are made up of amino acid residues. Post-translational modifications such as phosphorylations and glycosylations are usually also considered a part of the primary structure, and cannot be read from the gene. For example, insulin is composed of 51 amino acids in 2 chains. One chain has 31 amino acids, and the other has 20 amino acids. Secondary structure[edit] An a-helix with hydrogen bonds (yellow dots) Call/Whatsapp- 9166830064 PDE Notes Academy Page 6PDF Notes Academy Main article: Protein secondary structure Secondary structure refers to highly regular local sub-structures on the actual polypeptide backbone chain. Two main types of secondary structure, the a-helix and the B-strand or B-sheets, were suggested in 1951 by Linus Pauling et al.'5! These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups. They have a regular geometry, being constrained to specific values of the dihedral angles w and @ on the Ramachandran plot. Both the a- helix and the B-sheet represent a way of saturating all the hydrogen bond donors and acceptors in the peptide backbone. Some parts of the protein are ordered but do not form any regular structures. They should not be confused with random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure. Several sequential secondary structures may form a "supersecondary unit".[6 Tertiary structure[edit] Main article: Protein tertiary structure Tertiary structure refers to the three-dimensional structure created by a single protein molecule (a single polypeptide chain). It may include one or several domains. The a-helixes and B-pleated- sheets are folded into a compact globular structure. The folding is driven by the non-specific hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds. The disulfide bonds are extremely rare in cytosolic proteins, since the cytosol (intracellular fluid) is generally a reducing environment. Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Quaternary structure[edit] Main article: Protein quaternary structure Quaternary structure is the three-dimensional structure consisting of the aggregation of two or more individual polypeptide chains (subunits) that operate as a single functional unit (multimer). The resulting multimer is stabilized by the same non-covalent interactions and disulfide bonds as in tertiary structure. There are many possible quaternary structure organisations.'7) Complexes of two or more polypeptides (i.e. multiple subunits) are called multimers. Specifically it would be called a dimer if it contains two subunits, a trimer if it contains three subunits, a tetramer if it contains four subunits, and a pentamer if it contains five subunits. The subunits are frequently related to one another by symmetry operations, such as a 2-fold axis in a dimer. Multimers made up of identical subunits are referred to with a prefix of "homo-" and those made up of different subunits are referred to with a prefix of "hetero-", for example, a heterotetramer, such as the two alpha and two beta chains of hemoglobin. Domains, motifs, and folds in protein structure[edit] Protein domains. The two shown protein structures share a common domain (maroon), the PH domain, which is involved in phosphatidylinositol (3,4,5)-trisphosphate binding Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds. Call/Whatsapp- 9166830064 PDE Notes Academy Page 8PDF Notes Academy U Despite the fact that there are about 100,000 different proteins expressed in eukaryotic systems, there are many fewer different domains, structural motifs and folds. Structural domain{edit] A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins. Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, the "calcium-binding domain of calmodulin". Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera proteins. A conservative combination of several domains that occur in different proteins, such as protein tyrosine phosphatase domain and C2 domain pair, was called "a superdomain" that may evolve as a single unit.) Structural and sequence motifs[edit] The structural and sequence motifs refer to short segments of protein three-dimensional structure or amino acid sequence that were found in a large number of different proteins Supersecondary structure[edit] Tertiary protein structures can have multiple secondary elements on the same polypeptide chain. The supersecondary structure refers to a specific combination of secondary structure elements, such as B-a-B units or a helix-turn-helix motif. Some of them may be also referred to as structural motifs. Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Protein fold[edit] A protein fold refers to the general protein architecture, like a helix bundle, B-barrel, Rossmann fold or different "folds" provided in the Structural Classification of Proteins database." A related concept is protein topology. Protein dynamics and conformational ensembles[edit] Main article: Protein dynamics Proteins are not static objects, but rather populate ensembles of conformational states. Transitions between these states typically occur on nanoscales, and have been linked to functionally relevant phenomena such as allosteric signaling"? and enzyme catalysis.!") Protein dynamics and conformational changes allow proteins to function as nanoscale biological machines within cells, often in the form of multiprotein complexes.!! Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules, and dynein, which moves cargo inside cells towards the nucleus and produces the axonemal beating of motile cilia and flagella. "[I]n effect, the [motile cilium] is a nanomachine composed of perhaps over 600 proteins in molecular complexes, many of which also function independently as nanomachines...Flexible linkers allow the mobile protein domains connected by them to recruit their binding partners and induce long-range allostery via protein domain dynamics. "["9] Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy MD-based approach Ensemble iting the Combination of the replica into ‘xperinvental gata ‘he minal ensemble ee Deposition of the ensemble and the data Schematic view of the two main ensemble modeling approaches.!"41 Proteins are often thought of as relatively stable tertiary structures that experience conformational changes after being affected by interactions with other proteins or as a part of enzymatic activity. However, proteins may have varying degrees of stability, and some of the less stable variants are intrinsically disordered proteins. These proteins exist and function in a relatively ‘disordered’ state lacking a stable tertiary structure. As a result, they are difficult to describe by a single fixed tertiary structure. Conformational ensembles have been devised as a way to provide a more accurate and 'dynamic' representation of the conformational state of intrinsically disordered proteins. !"5Il"41 Protein ensemble files are a representation of a protein that can be considered to have a flexible structure. Creating these files requires determining which of the various theoretically possible protein conformations actually exist. One approach is to apply computational algorithms to the protein data in order to try to determine the most likely set of conformations for an ensemble file. There are multiple methods for preparing data Call/Whatsapp- 9166830064 PDF Notes Academy Page 11PDF Notes Academy for the Protein Ensemble Database that fall into two general methodologies — pool and molecular dynamics (MD) approaches (diagrammed in the figure). The pool based approach uses the protein’s amino acid sequence to create a massive pool of random conformations. This pool is then subjected to more computational processing that creates a set of theoretical parameters for each conformation based on the structure. Conformational subsets from this pool whose average theoretical parameters closely match known experimental data for this protein are selected. The alternative molecular dynamics approach takes multiple random conformations at a time and subjects all of them to experimental data. Here the experimental data is serving as limitations to be placed on the conformations (e.g. known distances between atoms). Only conformations that manage to remain within the limits set by the experimental data are accepted. This approach often applies large amounts of experimental data to the conformations which is a very computationally demanding task.!"4) The conformational ensembles were generated for a number of highly dynamic and partially unfolded proteins, such as Sic1/Cdc4,""9 p15 PAF,!"7] MKK7,!"®l Beta- synuclein!) and P2710! Protein folding[edit] This section needs expansion. You can help by adding to it. (April 2019) Main article: Protein folding Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy As it is translated, polypeptides exit the ribosome mostly as a random coil and folds into its native state.!1I22] The final structure of the protein chain is generally assumed to be determined by its amino acid sequence (Anfinsen's dogma).2*) Protein stability[edit] Main article: Equilibrium unfolding Thermodynamic stability of proteins represents the free energy difference between the folded and unfolded protein states. This free energy difference is very sensitive to temperature, hence a change in temperature may result in unfolding or denaturation. Protein denaturation may result in loss of function, and loss of native state. The free energy of stabilization of soluble globular proteins typically does not exceed 50 kJ/mol. [s#etion needed] Taking into consideration the large number of hydrogen bonds that take place for the stabilization of secondary structures, and the stabilization of the inner core through hydrophobic interactions, the free energy of stabilization emerges as small difference between large numbers.'41 Protein structure determination[edit] Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Examples of protein structures from the PDB Rate of Protein Svucture Determination (Log Scale) 3 Number of New Structres Per Year Rate of Protein Structure Determination by Method and Year Around 90% of the protein structures available in the Protein Data Bank have been determined by X-ray crystallography.5! This method allows one to measure the three-dimensional (3-D) density distribution of electrons in the protein, in the crystallized state, and thereby infer the 3-D coordinates of all the atoms to be determined to a certain resolution. Roughly 9% of the known protein structures have been obtained by nuclear magnetic resonance (NMR) techniques. [ton needed! For larger protein complexes, cryo-electron microscopy can determine protein structures. The resolution is typically lower than that of X- ray crystallography, or NMR, but the maximum resolution is steadily increasing. This technique is still a particularly valuable for very large protein complexes such as virus coat proteins and amyloid fibers. General secondary structure composition can be determined via circular dichroism. Vibrational spectroscopy can also be used to characterize the conformation of peptides, polypeptides, and Call/Whatsapp- 9166830064 PDF Notes Academy Page 14PDF Notes Academy U proteins.!25| Two-dimensional infrared spectroscopy has become a valuable method to investigate the structures of flexible peptides and proteins that cannot be studied with other methods.|27II28) 4 more qualitative picture of protein structure is often obtained by proteolysis, which is also useful to screen for more crystallizable protein samples. Novel implementations of this approach, including fast parallel proteolysis (FASTpp), can probe the structured fraction and its stability without the need for purification.!2°1 Once a protein's structure has been experimentally determined, further detailed studies can be done computationally, using molecular dynamic simulations of that structure.'9 Protein structure databases[edit] A protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way. Data included in protein structure databases often includes 3D coordinates as well as experimental information, such as unit cell dimensions and angles for x-ray crystallography determined structures. Though most instances, in this case either proteins or a specific structure determinations of a protein, also contain sequence information and some databases even provide means for performing sequence based queries, the primary attribute of a structure database is structural information, whereas sequence databases focus on sequence information, and contain no structural information for the majority of entries. Protein structure databases are critical for many efforts in computational biology such as structure based drug design, both in developing the computational methods used and in providing a large experimental dataset used by some methods to provide insights about the function of a protein.!1! Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Structural classifications of proteins[edit] Protein structures can be grouped based on their structural similarity, topological class or a common evolutionary origin. The Structural Classification of Proteins database'*"] and CATH database!**! provide two different structural classifications of proteins. When the structural similarity is large the two proteins have possibly diverged from a common ancestor, and shared structure between proteins is considered evidence of homology. Structure similarity can then be used to group proteins together into protein superfamilies.'*! If shared structure is significant but the fraction shared is small, the fragment shared may be the consequence of a more dramatic evolutionary event such as horizontal gene transfer, and joining proteins sharing these fragments into protein superfamilies is no longer justified.!*4] Topology of a protein can be used to classify proteins as well. Knot theory and circuit topology are two topology frameworks developed for classification of protein folds based on chain crossing and intrachain contacts respectively. Computational prediction of protein structure[edit] Main article: Protein structure prediction The generation of a protein sequence is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed.'4! Ab initio prediction methods use just the sequence of the protein. Threading and homology modeling methods can build a 3-D model for a protein of unknown structure from experimental structures of evolutionarily-related proteins, called a protein family. Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Nucleic acid Nucleic acids RNA (left) and DNA (right). Nucleic acids are biopolymers, macromolecules, essential to all known forms of life.!"] They are composed of nucleotides, which are the monomers made of three components: a 5-carbon sugar, a phosphate group and a nitrogenous base. The two main classes of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). If the sugar is ribose, the polymer is RNA; if the sugar is the ribose derivative deoxyribose, the polymer is DNA. Nucleic acids are naturally occurring chemical compounds that serve as the primary information-carrying molecules in cells and make up the genetic material. Nucleic acids are found in abundance in all living things, where they create, encode, and then store information of every living cell of every life-form on Earth. In turn, they function to transmit and express that information inside and outside the cell nucleus to the interior operations of the cell and ultimately to the next generation of each living organism. The encoded information is contained and conveyed via the nucleic acid sequence, which provides the ‘ladder-step' ordering of nucleotides within the molecules of RNA Call/Whatsapp- 9166830064 PDF Notes Academy Page 17PDF Notes Academy MCQ Molecules and their interactions relevant to biolo; Structure of molecules, chemical bonds and principles of biophysical chemist 1. Which of the following element is least abundant in our body? (a) Carbon (b) Oxygen (c) Phosphorus (d) Hydrogen Answer : 2. A polar molecule (a)is slightly negative at one end and slightly positive at the other end. (b) has an extra electron, giving it a negative charge. (c) has an extra neutron, making it weigh more. (d) has covalent bonds. Answer :- a 3. Which of the following property is not related to water? (a) High dielectric constant. (b) Dipolar nature. (c) Bond angle of 104.5 (d) Low heat of vaporization Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Answer :- d 4, Which of the following statements are correct? P. Polarity of water makes it an excellent solvent. Q. Water has high tensile strength. R. Cohesive property of water is due to H-bonding. S. Water has high dielectric constant. (a)P ands (b)Qand R. (©)Q, Rand $ (dP, Q, Rand S Answer :- d 5. Which non-covalent bond is responsible for the high melting and boiling points of water? (a) H-bond (b) van der Waals force (c) Hydrophobic force (d)Coyalent bond Answer := a 6. In which of the following systems is the entropy the greatest? (a) Water vapour (b) Liquid water at pH 7.0 and 37°C (c) Supercooled water (liquid water at a temperature less than 0°C) (d)Ice Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Answer :- a 7. If AG of the reaction A - B is -3.0 kcal/mol, which of the following statement is correct? (a) The reaction will proceed spontaneously from left to right at the given conditions. (b)The reaction will proceed spontaneously from right to left at standard conditions. (c) The equilibrium constant favors the formation of B over the formation of A. (d) The value of AG is also negative. Answer : 8. Which of the following is false? If the pH of a solution of HA, which dissociates to H* + A’, equals the pk,, then (a) the pH of the solution is 7. (b)the concentration of the acid form of the compound [HA] equals the concentration of the dissociated form of the compound [A]. (c) the solution has a greater capacity for buffering than at any other pH. (d)the hydrogen ion concentration is equal to describing the acid, HA = H* +A”. Answer :- a 9. Ifa reaction is at equilibrium, the free energy, AG change is (a1 (b)0 (©) 10 (0.1 Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Answer :- b 10.If for the biochemical reaction A — B, AH <0 and AS > 0, then (a) the reaction is spontaneous. (b) the reaction is endothermic. ()AG = 0. (d) the disorder in the system will decrease if the reaction proceeds, Answer :- a 11. The ion product of water (a)is independent of temperature (b)has a numerical value of 1x10-14 at 25°C. (©) is the equilibrium constant for the reaction HOH (d) requires that [H*] and [OH’] always be identi Answer :- b 12. Which of the following is part of the first law of thermodynamics? (a) Energy cannot be created or destroyed. (b) The entropy of the universe is decreasing. (c) The entropy of the universe is constant. (@) Energy cannot be transferred or transformed. Answer : Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Unit 13.Consider a 51-residue long protein containing only 100 bonds about which rotation can occur. Ass 3 orientations per bond are possible. Based on these assumptions, how many conformations will be for this protein? (a3 (b) 100° 3" (d)51 x 100 x3 Answer :- a 14. The isoelectric point of a protein is defined as (a) the pH at which the net charge on the molecule is zero. (b) the pH at which all groups are protonated. (©) the pH at which all groups are unprotonated. (d)the pH at which each acidic group is protonated and each basic group is unprotonated. Answer :- a 15.Which one of the following is the major force of attraction that stabilizes the three dimensional structure of globular proteins? (a) Peptide bond (b) van der Waals interaction (c) Hydrogen bond (d) Hydrophobic force Answer :- d 16.Which of the following amino acids have side chains that are negatively charged under physiological conditions (i.e. near pH 7)? (a) Asp Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy (b) His (Tp (Cys Answer : 17.If a polypeptide has 400 amino acid residues, what is its approximate mass? (a) 11,000 daltons (b) 44,000 daltons (©) 22,000 daltons (d) 88,000 daltons Answer :- b 18.Which of the following amino acid residue is likely to be found on the inside of a water-soluble protein (a) Arg (b) His, (©) Asp @lle Answer :- d 19.[f the average molecular weight of one amino acid is 128, the molecular weight of a linear oligopeptide made up of 10 amino acids is approximately (a) 938 (b) 1100 (©) 876 (d)744 Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Answer :- b 20.A petide has the sequence Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly. What is. the net charge of the molecule at pH 11? (a) +2 (b)-2 (©)0 (d)-1 Answer :- d 21 Isoelectric point of the enzyme ribonuclease is 9.3. It was observed that at this point there are 10 positively charged and 10 negatively charged side chains of amino acids. When the enzyme solution was titrated with HCI to give a pH of 3, it was observed that 2 ionized glutamic acid and 1 ionized aspartic acid side chain got protonated. The net charge on the enzyme at pH 3 would, therefore, be (a) +2 (b)+3 (c)+7 (d)+97 Answer :- b 22.In the a-helix the hydrogen bonds (a) are perpendicular to the axis of the helix. (b) occur mainly between electronegative atoms of the R groups (c) occur mainly between electronegative atoms of the backbone. (d) occur only between some of the amino acids of the helix. Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Answer : 23. The rise per residue of a-helix is about 1.5 A. A protein spans 4 nm bilayer 7 times through its transmembrane a-helical domain. Approximately, how many amino acid residues constitute the transmembrane domain of the protein? (a) 105 (b) 450 (©)30 (d) 190 Answer :- d 24.The a-helix secondary structure of polypeptide P. is maintained by hydrogen bonding between amino acid side chains. Q. is stabilized by H-bonds that lie parallel to the helix axis and point in the same direction. R. is stabilized by H-bonds between the amino and carboxyl termini of the polypeptide chain S. is stabilized by H-bonds between backbone N-H and C=O groups of polypeptide chains. (a)P and Q (b)P and R (©) Qand S (@)QandR Answer :- ¢ 25.A cyclic peptide containing the sequence D-valine, L-lactate, L-valine and D-hydroxyisovalerate repeated three es forms a complex with K+ ions which is highly soluble in lipid bilayers. The structure of the molecule is likely to be (a) hydrophilic side chains exposed on the perimeter of the molecule. Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy (b) hydrophobic groups buried inside the molecule. (©) hydrophobic side chains exposed around the perimeter of the molecule. (d)none of the above. Answer :- c 26.Upon studying the folding of RNase A, Anfinsen concluded that (a)protein denaturation and renaturation do not violate basic. laws of thermodynamics. (b)a cysteine residue can form a disulfide bond only with the nearest cysteine residue, (c)attainment of native conformation by a protein is a spontaneous process, (d) once a protein is denatured, it can only be partially renatured, Answer :- c 27.Myoglobin shows a hyperbolic response, while hemoglobin shows a sigmoidal response for Which of the following statements are true with respect to this observation? P. Hemoglobin binds 2,3-BPG while myoglobin does not. Q. Hemoglobin exists in two different conformational states while myoglobin does not. R, Hemoglobin is a tetramer while myoglobin is a monomer. S. Hemoglobin is present in RBCs while myoglobin is present in the muscle. (a) Rand S (b)b. S and P (©)Pand Q (d)Qand R. Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy Answer :- d 28.According to the sequential model for allosteric proteins, which of the following statement is true for hemoglobin? (a) Each of the four subunits in hemoglobin changes one at a time from the low affinity state to affinity state. (b)The a-subunits followed by the B-subunits change from the low affinity to the high affinity state (c) The B-subunits followed by the a-subunits change from the low affinity to the high affinity state (d)Each of the four subunits in the hemoglobin tetramer is either in a low affinity state or a high affinity state. Answer : 29, When hemoglobin is converted from the deoxy form to oxyhemoglobin (a) it becomes more acidic and releases protons. (b) carbamino formation is promoted. (c) binding of BPG is favored. (d) bound NO is transferred to glutathione. Answer :- a 30.Why is hemoglobin ideally suited as an oxygen transporter instead of myoglobin? (a) Hemoglobin has higher binding affinity for oxygen at high oxygen tension (b) Hemoglobin gives up its oxygen more readily at low oxygen tension. (c) Binding of oxygen to hemoglobin is non-cooperative. (d) Myoglobin undergoes a conformational change after oxygen binding such that oxygen cannot be released in tissues. Answer :- b Call/Whatsapp- 9166830064 PDF Notes AcademyPDF Notes Academy 31.Which of the following statements is false? (a) Proteins tend to be least soluble in water at their isoelectric point. (b) Sickle cell Hb and normal Hb have same value of negative charge. (©) Amino acids are made visible on the chromatogram by treatment with ninhydrin. (d) The net charge on an amino acid is a function of the pH of the solution. Answer :- b 32.Which of the following statements about the structures of water-soluble proteins, such as myoglobin, die not true? 1. They contain tightly packed amino acids in their interior. 2. Most of their nonpolar residues face the aqueous solvent. 3. The main chain NH and CO groups ate often involved in H-bonded secondary structures in the in these prote 4, Polar residues such as His may be found in the interior of these proteins if the residues have specificiu 5. All of these proteins contain beta sheet structural motifs. (a)2 and 4 (b)2 and 5 () 1,2 and 4 (d)2, 3 and 5 Answer :- b 33.Which of the following statements are correct about collagen? P. Extremely rich in proline and glycine. Q.A double helix, where two a-chains are wrapped around one another in a rope-like structure, Call/Whatsapp- 9166830064 PDF Notes Academy