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Protein

Protein metabolism

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Hasen umer
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0% found this document useful (0 votes)
18 views8 pages

Protein

Protein metabolism

Uploaded by

Hasen umer
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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ae fen and named beginning with al residue on the left residue on the TLis a noncovalent linkage formed from two cysteine residues jary structure of proteins 3 Which of the following statement about elastin is NOT correct? a) Some tissues such as ligaments and arterial blood vessels have large us component of skin, bone, tendon, cartilage and teeth, ) The — peptide chain of elastin is rich in glycine, alanine and valine. @) They are very flexible and eesily extended. SE Myoglobin a) is a globular protein whose shape is secondary structure ), is a fibrous protein whose shape is tertiary structure -@) about 80% of its polypeptide chain folded into 6 stretches of a-helix -an bind only one oxygen molecule _ hemoglobinopathies 2 Sickle cell anemia occurs duc to substitution of valine by lysine 'p)_o-Thalassemias occurs doe to synthesis of beta-globin chains is decreased or wi gontains thes ft is rich in the am”) no ae , it keratin Tris a connective tissue proteln with rubber his ‘present tal struct €). {contains about 33% of the amino acié BY @) Itcontains heme group ber-like propetti protein is called 1L- The sequence of amino acids in 2 ~aprcrre Or pro‘ ‘Structure of protein ©) eit structure of protein dé) Quaternary structure ¢ of protein fp denatured remain, ermanently aicwered) Taffect the tertiary structure of protein ae the 5 nts cause hydro}ysis of protein into. ae acids see jon causes a change in thé priprary structure of protein ids is a branched ¢ amino acid 5 Denaturing d) Reversible denaturati 13- One of the following amino aci ‘amino acids have the same basic structure except amino acids are 2 polar in their side chains - prep On poy amino acids EXCEPT. Denaturation of a protein | involves alteration of eee c quintemiary levels of its structure > F ) THE primary secondary, or tertiary, levels of its structure ») The primary structure only ) The primary and tertiary stracture S- Edman degrada ation, is a method “FAY Segue sing aming acl B) Finger print detection ©) Peptide bond analysis 1D) Disulfide bond break down ten al-Antitrypsin 5 AA) It allows elastase to break elastin B) Its deficiency may cause scurvy C) Ic is the basic unit of collagen structure : D) Its deficiency in lungs may result in breathing bei! fo Amino aside are isle aserding fo —_—_ mt = oo) Senne het Me ‘of the following is considered as an aromatic amino acid? @ a : Serine Riedy ov : D) Arginine “pasit Ue) 44: One of the following is an essential amino acid A) Glycine —— 1) Pratalanine J C) Aspartate D) Glutamate ming acids can act.as both an acid and a base due to ce of the amino and carboxyl functional g groups 8). The amino Raa group C) The carboxy! functional group 5) The optical activity For the peptide glycylseryltryptophylarginine Tt contains two indroxyl |-containing amino acids “€Xd)_ c-Lelix and B-sheet are stabilized by covalent bonds 39- About disulfide bonds e) Itise ent linkage formed from two cysteine residues “fh ison i iclife of proteins ) g) It cannot be found in keratin h) Itisa covalent bond formed from two methionine residues 40- About glycine a) Itis optically active amino acid b) It can be found in high concentration in myoglobin 6) Its one of the branched chain amino acid itis gh concentratio gen 41- Which one of the following amino acids has a secondary amino group? a). Alanine rue. b) Glycine : Sy Profine) 4) Methionine 42- About collagen ~~) Wis composed of 3 polypeptide chains held Together by hydrogen bonds. ) 'b} Cysteine is important ir ng the triple-helical structure of collagen ©) Proline and alanine are the most abundant amino acids found in collagen ) {lis rich in disulfide bonds 43- Abour hemoglobin a)_Heroglobin A is composed of two alpha and two gamma chains gop) The four subunits of hemoglobin are held by noncovalent bor c) Hemogiobin S is a normal structure found in adults : © BERa) ts function is transport and storage oF oxygen in skeletal muscles” 44. One of the following is not allosteric effector that affect biriding of oxygen to hemogiobin a) Partia! pressure of oxygen b) Partial pressure of carbon dioxide + | co) pH d)_3- phosphowlycerate 45- About myoglobin ae sists of a two polypeptide chains ‘Gy Teenie “ST ihe myoglobiirls coispesed of nonpolar amino acts: ) ‘Uncharged amit nO aGid are located on the surface € 4) About 0% ots polyp : inopathies . ae link by ghinetonte 46- About hemoglobi i due to substitution of valine by glutamate S Sickle cell ae er, duc fo symmhesis of beterobln chains is decreased a-Thalassemias ¢ Cee ne AEs ; ypeptide chain Folded into 5 stretches of w-helix 48- Tyrosine is a) Ketogenic amino acid only p) Glucogenic aminoacid only (@), Bath glucogenic and hetogenic amino acid )) Essential amino acid ae 49- About Zyvitterion a) It is the one polar form of amino acid bb) Itis electrically neutral, net charge is positive ¢) Itis electrically ngutral, net charge is negative > JH): It is electrically neutral, net charge ey are Tend ia sone inplant and bacterial cell wells “b) Chey are found in all proteins that form humnan body <) They are nonessential amino acids to human 4) They can be present in collagen and elastin $1- Ornithine and citrulline are Paes ad oJ Ue MEDICINE AP _ plies Jolaadd ols sal Keep walking towards your goal tme/medicine_46

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