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| Title Name | IGNOU BBCCT 105 SOLVED ASSIGNMENT HINDI |
|---|---|
| Type | Soft Copy (E-Assignment) .pdf |
| University | IGNOU |
| Degree | BACHELOR DEGREE PROGRAMMES |
| Course Code | BSCBCH |
| Course Name | B.Sc. Honours in Biochemistry |
| Subject Code | BBCCT 105 |
| Subject Name | Proteins |
| Year | 2026 |
| Session | |
| Language | English Medium |
| Assignment Code | BBCCT-105/Assignmentt-1//2026 |
| Product Description | Assignment of BSCBCH (B.Sc. Honours in Biochemistry) 2026. Latest BBCCT 105 2026 Solved Assignment Solutions |
| Last Date of IGNOU Assignment Submission | Last Date of Submission of IGNOU BBCCT-105 (BSCBCH) 2026 Assignment is for January 2026 Session: 30th September, 2026 (for December 2026 Term End Exam). Semester Wise January 2026 Session: 30th March, 2026 (for June 2026 Term End Exam). July 2026 Session: 30th September, 2026 (for December 2026 Term End Exam). |
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Ques 1.
अमीनो एसिड को उनकी साइड चेन की प्रकृति के आधार पर वर्गीकृत करें और हाइड्रोफोबिक, ध्रुवीय और चार्ज वाले अमीनो एसिड के गुणों का वर्णन करें।
Ques 2.
समझाएँ कि प्रोटीन संरचना की विविधता (मल्टीमेरिक, संयुग्मित और मेटालोप्रोटीन) उनके जैविक कार्यों की विस्तृत श्रृंखला में कैसे योगदान करती है।
Ques 3.
सेलुलर स्रोतों से प्रोटीन के घुलने और निकालने में शामिल सिद्धांतों का वर्णन करें।
Ques 4.
विभिन्न प्रोटीन निष्कर्षण विधियों की तुलना करें और झिल्ली-बद्ध प्रोटीन को अलग करने के लिए एक उपयुक्त तकनीक के चुनाव को सही ठहराएँ।
Ques 5.
प्रोटीन शुद्धिकरण में अमोनियम सल्फेट प्रभाजन और डायलिसिस के सिद्धांत को समझाएँ।
Ques 6.
र्णन करें कि शुद्धिकरण के दौरान प्रोटीन को केंद्रित और स्थिर करने के लिए विलायक प्रभाजन और लियोफिलाइजेशन का उपयोग कैसे किया जाता है।
Ques 7.
आयन-एक्सचेंज, जेल निस्पंदन और एफिनिटी क्रोमैटोग्राफी के सिद्धांतों का वर्णन करें
Ques 8.
कच्चे प्रोटीन अर्क से एक एंजाइम को अलग करने के लिए क्रोमैटोग्राफिक तकनीकों का उपयोग करके एक शुद्धिकरण रणनीति डिजाइन करें
Ques 9.
प्रोटीन शुद्धता और आणविक भार निर्धारित करने के लिए उपयोग की जाने वाली विधियों का वर्णन करें।
Ques 10.
समझाएँ कि जटिल प्रोटीन मिश्रणों का विश्लेषण करने के लिए SDS & PAGE आइसोइलेक्ट्रिक फोकसिंग और 2-D इलेक्ट्रोफोरेसिस का उपयोग कैसे किया जा सकता है
Ques 11.
प्रोटीन अनुक्रमण के लिए एडममैन डिग्रेडेशन के सिद्धांत को समझाएँ।
Ques 12.
वर्णन करें कि ओवरलैपिंग पेप्टाइड कैसे उत्पन्न होते हैं और प्रोटीन के पूर्ण अमीनो एसिड अनुक्रम को निर्धारित करने के लिए उनका उपयोग कैसे किया जाता है
Ques 13.
प्रोटीन के मास स्पेक्ट्रोमेट्रिक विश्लेषण के मूल सिद्धांत का वर्णन करें।
Ques 14.
समझाएँ कि रामचंद्रन प्लॉट का उपयोग प्रोटीन माध्यमिक संरचना की भविष्यवाणी और सत्यापन के लिए कैसे किया जाता है।
Ques 15.
प्रोटीन संरचना निर्धारण में उपयोग किए जाने वाले एक्स-रे विवर्तन और NMR स्पेक्ट्रोस्कोपी के सिद्धांतों का वर्णन करें।
Ques 16.
चर्चा करें कि प्रोटीन फोल्डिंग में दोष अल्जाइमर रोग और प्रियन विकारों जैसी बीमारियों को कैसे जन्म देते हैं।
Ques 17.
प्रोटीन अनुक्रम और संरचना डेटाबेस के संगठन और सामग्री का वर्णन करें
Ques 18.
समझाएँ कि कोलेजन और एक्टिन जैसे संरचनात्मक प्रोटीन सेलुलर अखंडता और गति में कैसे योगदान करते हैं।
Ques 19.
ऑक्सीजन पृथक्करण वक्रों की सहायता से हीमोग्लोबिन और मायोग्लोबिन के ऑक्सीजन–बाध्यकारी गुणों का वर्णन करें
Ques 20.
मांसपेशियों के संकुचन के दौरान ATP–संचालित एक्टिन–मायोसिन इंटरैक्शन के आणविक तंत्र को समझाएँ।
Ques 21.
Classify amino acids based on the nature of their side chains and describe the properties of hydrophobic, polar, and charged amino acids.
Ques 22.
Explain how the diversity of protein structure (multimeric, conjugated, and metalloproteins) contributes to their wide range of biological functions.
Ques 23.
Describe the principles involved in solubilization and extraction of proteins from cellular sources.
Ques 24.
Compare different protein extraction methods and justify the choice of a suitable technique for isolating a membrane-bound protein.
Ques 25.
Explain the principle of ammonium sulphate fractionation and dialysis in protein purification.
Ques 26.
Describe how solvent fractionation and lyophilization are used to concentrate and stabilize proteins during purification.
Ques 27.
Describe the principles of ion-exchange, gel filtration, and affinity chromatography.
Ques 28.
Design a purification strategy using chromatographic techniques to isolate an enzyme from a crude protein extract.
Ques 29.
Describe methods used for determining protein purity and molecular weight.
Ques 30.
Explain how SDS-PAGE, isoelectric focusing, and 2-D electrophoresis can be used to analyze complex protein mixtures.
Ques 31.
Explain the principle of Edman degradation for protein sequencing.
Ques 32.
Describe how overlapping peptides are generated and used to determine the complete amino acid sequence of a protein.
Ques 33.
Describe the basic principle of mass spectrometric analysis of proteins.
Ques 34.
Explain how Ramachandran plots are used to predict and validate protein secondary structure.
Ques 35.
Describe the principles of X-ray diffraction and NMR spectroscopy used in protein structure determination.
Ques 36.
Discuss how defects in protein folding lead to diseases such as Alzheimer's disease and prion disorders.
Ques 37.
Describe the protein sequence and structure databases.
Ques 38.
Explain how structural proteins such as collagen and actin contribute to cellular integrity and movement.
Ques 39.
Describe the oxygen-binding properties of haemoglobin and myoglobin with the help of oxygen dissociation curves.
Ques 40.
Explain the molecular mechanism of ATP-driven actin-myosin interaction during muscle contraction.
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| Course Name | B.Sc. Honours in Biochemistry |
| Course Code | BSCBCH |
| Programm | BACHELOR DEGREE PROGRAMMES Courses |
| Language | English |
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