112. Protein Structure & Function

You are here: Home / 112. Protein Structure & Function

 

112. Protein Structure & Function

 

 

CATEGORY: Diet Nutrition Supplementation – 500 Courses

COURSE NUMBER: 112

FEES: 555/- INR only

CERTIFICATE VALIDITY: Lifetime

CERTIFICATES DELIVERY: In 48 hours

BOOKS/ MANUALS: Pages

Syllabus

Part I Proteins
1 Amino Acids……………………………………………………….. 3
1.1 Basic Structure of Amino Acids………………………………. 3
1.2 The Isoelectric Point …………………………………………. 4
1.3 The One-Letter Code …………………………………………. 9
1.4 Biological Function of Amino Acid Variety …………………… 10
1.5 Exercises…………………………………………………….. 12
1.5.1 Problems ……………………………………………. 12
1.5.2 Solutions ……………………………………………. 12
Reference …………………………………………………………… 13
2 Protein Structure ………………………………………………….. 15
2.1 Primary Structure…………………………………………….. 15
2.1.1 Protein Sequences and Evolution …………………….. 18
2.2 Secondary Structure ………………………………………….. 20
2.2.1 The ̨-Helix …………………………………………. 22
2.2.2 ˇ-Strand …………………………………………….. 24
2.2.3 The PII (syn.: Poly-Pro or Polypeptide II) Helix ………. 28
2.2.4 Hairpin Turns ……………………………………….. 30
2.2.5 Rare Structures………………………………………. 31
2.2.6 Coils………………………………………………… 32
2.3 Tertiary Structure …………………………………………….. 32
2.3.1 Classification of Proteins by Folding Pattern………….. 34
2.4 Quaternary Structure …………………………………………. 37
2.5 Further Aspects of Protein Structure ………………………….. 38
2.5.1 LEVINTHAL’s paradox: ……………………………… 38
2.5.2 Energetics and Kinetics of Protein Folding …………… 40
2.5.3 Morpheeins …………………………………………. 41
2.5.4 Molecular Chaperones and Chaperonins ……………… 42
2.5.5 Protein Denaturation…………………………………. 42
2.5.6 Protein Folding ……………………………………… 43

2.6 Posttranslational Modifications of Proteins ……………………. 47
2.6.1 Glycosylation ……………………………………….. 47
2.6.2 Glucation ……………………………………………. 49
2.6.3 Disulphide Bond Formation………………………….. 50
2.6.4 Proteolysis ………………………………………….. 51
2.6.5 Hydroxylation……………………………………….. 52
2.6.6 Phosphorylation/Dephosphorylation …………………. 53
2.6.7 Acetylation/Deacetylation……………………………. 53
2.6.8 Methylation/Demethylation ………………………….. 54
2.6.9 Addition/Removal of Hydrophobic Tails……………… 55
2.6.10 S-Nitrosylation………………………………………. 55
2.6.11 ADP-Ribosylation …………………………………… 55
2.6.12 Deamidation ………………………………………… 55
2.6.13 AMPylation (Adenylylation)…………………………. 57
2.6.14 Transfer of Peptides …………………………………. 57
2.7 The Relationship Between Protein Structure
and Function: Green Fluorescent Protein ……………………… 59
2.8 Exercises…………………………………………………….. 61
2.8.1 Problems ……………………………………………. 61
2.8.2 Solutions ……………………………………………. 62
References………………………………………………………….. 62
3 Proteins in the Lab ………………………………………………… 65
3.1 Protein Purification …………………………………………… 65
3.1.1 Homogenisation and Fractionisation of Cells
and Tissues………………………………………….. 65
3.1.2 Precipitation Methods ……………………………….. 66
3.1.3 Chromatography …………………………………….. 67
3.1.4 Electrophoresis ……………………………………… 71
3.1.5 Membrane Proteins ………………………………….. 73
3.2 Determination of Protein Concentration ………………………. 76
3.3 Protein Sequencing …………………………………………… 78
3.3.1 Edman Degradation …………………………………. 78
3.3.2 Mass Spectrometry ………………………………….. 79
3.3.3 Phylogenetic Trees ………………………………….. 83
3.4 Synthesis of Peptides…………………………………………. 85
3.5 How Do We Determine Secondary Structure? …………………. 85
3.5.1 X-Ray Crystallography ………………………………. 86
3.5.2 Electron Microscopy ………………………………… 87
3.5.3 Nuclear Magnetic Resonance ………………………… 87
3.5.4 Computer Predictions ……………………………….. 88
3.6 Exercises…………………………………………………….. 89
3.6.1 Problems ……………………………………………. 89
3.6.2 Solutions ……………………………………………. 91
References………………………………………………………….. 91

Part II Enzymes
4 Enzymes Are Biocatalysts …………………………………………. 97
4.1 The Nature of Catalysis ………………………………………. 97
4.1.1 A Brief History of Enzymology ……………………… 98
4.2 Enzyme Classification and EC Code ………………………….. 101
4.2.1 Chemical and Biological Direction of a Reaction……… 104
4.3 Inherited Diseases of Metabolism …………………………….. 104
4.4 Exercises…………………………………………………….. 109
4.4.1 Problems ……………………………………………. 109
4.4.2 Solutions ……………………………………………. 109
References………………………………………………………….. 110
5 Enzyme Kinetics and Mechanism …………………………………. 111
5.1 The HENRI–MICHAELIS–MENTEN Equation …………………. 111
5.1.1 Efficiency Constant and Catalytic Perfection …………. 117
5.1.2 Application: Forensic Determination of Blood
Alcohol Concentration ………………………………. 119
5.1.3 Linearisation of the HMM-Equation …………………. 120
5.1.4 Experimental Pitfalls ………………………………… 123
5.1.5 Environmental Influences on Enzyme Activity ……….. 126
5.2 Enzymes with Several Substrates……………………………… 126
5.2.1 Nomenclature ……………………………………….. 127
5.2.2 How Do We Determine the Mechanism
of Multisubstrate Enzymes?………………………….. 128
5.3 Enzyme Precursors and Their Activation ……………………… 129
5.4 The Coupled Spectrophotometric Assay of WARBURG ………… 130
5.5 How Do Enzymes Work? …………………………………….. 131
5.5.1 Molecular Mechanism of Serine-Proteases
and -Esterases……………………………………….. 133
5.6 Exercises…………………………………………………….. 135
5.6.1 Problems ……………………………………………. 135
5.6.2 Solutions ……………………………………………. 137
References………………………………………………………….. 139
6 Inhibition and Inactivation of Enzymes……………………………. 141
6.1 Enzyme Inhibition……………………………………………. 141
6.2 Competitive Inhibition ……………………………………….. 142
6.3 Uncompetitive Inhibition …………………………………….. 147
6.4 Noncompetitive Inhibition ……………………………………. 148
6.5 Partial Inhibition……………………………………………… 151
6.6 Inactivation of Enzymes ……………………………………… 154
6.7 Exercises…………………………………………………….. 157
6.7.1 Problems ……………………………………………. 157
6.7.2 Solutions ……………………………………………. 160
References………………………………………………………….. 161

7 Hæmoglobin and Myoglobin: Cooperativity ………………………. 163
7.1 Structure …………………………………………………….. 165
7.2 Oxygen Binding and Cooperativity …………………………… 165
7.2.1 Functional Significance of Cooperativity……………… 167
7.2.2 Mechanism of Cooperativity …………………………. 168
7.2.3 Other Factors Involving Oxygen Affinity
of Hæmoglobin ……………………………………… 173
7.3 Hæmoglobin Related Diseases ……………………………….. 176
7.3.1 Subunit Composition of Human Hæmoglobin ………… 176
7.3.2 Inherited Diseases Relating to Hæmoglobin ………….. 177
7.4 Exercises…………………………………………………….. 183
7.4.1 Problems ……………………………………………. 183
7.4.2 Solutions ……………………………………………. 183
References………………………………………………………….. 183
8 Enzyme Kinetics: Special Cases……………………………………. 185
8.1 Activation Cascades………………………………………….. 185
8.2 Feedback-Networks ………………………………………….. 188
8.3 Multiple Phosphorylation …………………………………….. 190
References………………………………………………………….. 191
9 The Flow of Metabolites Through Metabolic Pathways……………. 193
9.1 Flux Control Theory …………………………………………. 194
9.1.1 Supply/Demand Analysis ……………………………. 197
9.1.2 Mechanism of Flux Control ………………………….. 197
References………………………………………………………….. 199
Part III Special Proteins
10 Protein Folding Diseases …………………………………………… 203
10.1 Intrinsically Disordered Proteins ……………………………… 203
10.1.1 Protein-Only Elements of Inheritance ………………… 205
10.2 Amyloidoses…………………………………………………. 206
10.2.1 Prion Proteins and Prion Diseases ……………………. 207
10.2.2 Neuronal Amyloidoses ………………………………. 213
10.2.3 Amyloidoses in Other Organs………………………… 218
10.2.4 Amyloidoses Secondary to Other Diseases …………… 220
10.3 Exercises…………………………………………………….. 221
10.3.1 Problems ……………………………………………. 221
10.3.2 Solutions ……………………………………………. 221
References………………………………………………………….. 222
11 Immunoproteins …………………………………………………… 225
11.1 Overview…………………………………………………….. 226
11.1.1 Cells of the Immune System …………………………. 227
11.2 Humoral Immunity: Immunoglobulins………………………… 231
11.2.1 Structure of Immunoglobulins ……………………….. 231

11.2.2 How Is the Large Number of Ig-Molecules Obtained? … 234
11.2.3 Time Course of Antibody Response ………………….. 241
11.2.4 Immunisation ……………………………………….. 244
11.2.5 Monoclonal Antibodies ……………………………… 246
11.2.6 Laboratory Uses of Antibodies ………………………. 247
11.3 Destroying Invaders: The Complement System ……………….. 249
11.3.1 How Is Complement Activated? ……………………… 251
11.3.2 What Does Complement Do? ………………………… 253
11.3.3 How Is Complement Inactivated?…………………….. 256
11.4 Cellular Immunity ……………………………………………. 258
11.4.1 The Major Histocompatibility Complex………………. 258
11.4.2 The T-Cell Receptor …………………………………. 267
11.5 Proteins Involved in Innate Immunity …………………………. 270
11.5.1 PAMP-Receptors ……………………………………. 270
11.5.2 Cytokines …………………………………………… 275
11.5.3 The Acute-Phase Response ………………………….. 277
11.5.4 Antibacterial Proteins ……………………………….. 278
11.6 Exercises…………………………………………………….. 281
11.6.1 Problems ……………………………………………. 281
11.6.2 Solutions ……………………………………………. 282
References………………………………………………………….. 283
12 Cell Skeleton ………………………………………………………. 287
12.1 The Microfilament……………………………………………. 288
12.1.1 Basic Actin Structure ………………………………… 288
12.1.2 Actin-Binding Proteins………………………………. 291
12.1.3 Functions of Actin …………………………………… 295
12.1.4 Actin-Networks……………………………………… 295
12.2 Microtubules…………………………………………………. 296
12.2.1 Microtubule Structure ……………………………….. 297
12.3 Intermediate Filament ………………………………………… 299
12.3.1 IF-Proteins Are Cell-Type Specific …………………… 300
12.3.2 Structure of Intermediate Filaments ………………….. 302
12.3.3 Intermediate Filaments and Cell Cycle ……………….. 303
12.3.4 Other Proteins Associated with Intermediate
Filaments……………………………………………. 303
12.4 Exercises…………………………………………………….. 304
12.4.1 Problems ……………………………………………. 304
12.4.2 Solutions ……………………………………………. 304
References………………………………………………………….. 304
13 Motor Proteins and Movement…………………………………….. 305
13.1 Myosin Moves Along Actin Filaments………………………… 305
13.1.1 Myosin Structure ……………………………………. 305
13.1.2 Myosin-II …………………………………………… 306

13.1.3 Myosin-I ……………………………………………. 310
13.1.4 Myosin-V …………………………………………… 311
13.2 Kinesin and Dynein Move Along Microtubules ……………….. 311
13.2.1 Kinesin Is Responsible for Anterograde
(Minus to Plus) Transport ……………………………. 311
13.2.2 Dynein Is Responsible for Retrograde (Plus to
Minus) Movement …………………………………… 313
13.3 Cilia and Flagella…………………………………………….. 313
13.3.1 Generic Structure of Cilia and Flagella ……………….. 313
13.3.2 Mechanism of Movement ……………………………. 315
13.3.3 Cilia and Flagella Start Growing at the Basal Body …… 317
13.4 The Mitotic Spindle ………………………………………….. 317
References………………………………………………………….. 322
14 Cell–Cell Interactions ……………………………………………… 323
14.1 Extracellular Matrix ………………………………………….. 323
14.1.1 Collagen…………………………………………….. 324
14.1.2 Elastin ………………………………………………. 331
14.2 Cell Adhesion Molecules …………………………………….. 335
14.3 Junctions…………………………………………………….. 337
14.3.1 Disintegrins …………………………………………. 339
14.4 Exercises…………………………………………………….. 339
14.4.1 Problems ……………………………………………. 339
14.4.2 Solutions ……………………………………………. 340
References………………………………………………………….. 340
15 Aiding in Folding: Molecular Chaperones and Chaperonins………. 343
15.1 Hsp70 Is an Example for Molecular Chaperones………………. 345
15.2 Other Heat Shock Proteins also Have Chaperone Activity ……… 350
15.2.1 Hsp90 ………………………………………………. 350
15.2.2 Small Heat Shock Proteins…………………………… 353
15.3 The GroEL/GroES-Foldosome Is an Example
for Molecular Chaperonins …………………………………… 354
15.4 Exercises…………………………………………………….. 357
15.4.1 Problems ……………………………………………. 357
15.4.2 Solutions ……………………………………………. 358
References………………………………………………………….. 358
Part IV Membrane Transport
16 Protein Transport Across Membranes …………………………….. 363
16.1 Structure of Membrane Components………………………….. 363
16.1.1 Membrane Lipid …………………………………….. 363
16.1.2 Membrane Proteins ………………………………….. 364
16.2 Transport of Proteins into Mitochondria ………………………. 368
16.2.1 The Mitochondrium in the Cell Cycle ………………… 368
16.2.2 Mitochondrial Proteins and Lipids……………………. 369

16.3 Synthesis and Sorting of Mitochondrial Proteins in the Cytosol… 371
16.4 Transfer of Protein into the ER Lumen………………………… 375
16.5 Folding and Quality Control of Membrane Proteins …………… 377
16.5.1 Posttranslational Modification in the ER ……………… 377
16.5.2 Glycosylation ……………………………………….. 379
16.5.3 Protein Quality Control in the ER ……………………. 385
16.6 Exercises…………………………………………………….. 387
16.6.1 Problems ……………………………………………. 387
16.6.2 Solutions ……………………………………………. 389
References………………………………………………………….. 389
17 Vesicular Transport in Eukaryotic Cells …………………………… 393
17.1 Two Models for Transport Between Compartments……………. 393
17.1.1 Maturation ………………………………………….. 393
17.1.2 Vesicular Transport ………………………………….. 395
17.1.3 Experimental Evidence ………………………………. 395
17.2 Clathrin ……………………………………………………… 395
17.2.1 Endocytosis, Membrane Protein Recycling,
and Transcytosis …………………………………….. 396
17.3 “-Coat Protein ……………………………………………….. 403
17.3.1 Vesicular Transport Between ER and GOLGI Stacks ….. 403
17.4 The Specificity of Membrane Fusion………………………….. 409
17.4.1 v-SNAREs and t-SNAREs …………………………… 409
17.4.2 Rab Proteins ………………………………………… 409
17.4.3 How Do Proteins Know Where They Belong? ………… 410
17.5 Other Vesicular Transport Pathways ………………………….. 412
17.5.1 Transport of Newly Synthesised Proteins
to Their Destination …………………………………. 412
17.5.2 Proteins Taken Up by the Cell ……………………….. 416
17.6 Exercises…………………………………………………….. 417
17.6.1 Problems ……………………………………………. 417
17.6.2 Solutions ……………………………………………. 418
References………………………………………………………….. 419
18 Transport of Solutes Across Membranes ………………………….. 421
18.1 Passive Diffusion …………………………………………….. 422
18.2 Transporters …………………………………………………. 423
18.2.1 Primary Active Transporters (Pumps) ………………… 424
18.2.2 Secondary Active Transporter (Cotransporter)………… 454
18.2.3 Facilitated Diffusion …………………………………. 458
18.3 Exercises…………………………………………………….. 465
18.3.1 Problems ……………………………………………. 465
18.3.2 Solutions ……………………………………………. 466
References………………………………………………………….. 467

Appendix A: Short Biographies of Scientists Mentioned in This Book …. 469
Appendix B: List of Symbols……………………………………………. 489
Appendix C: Greek Alphabet…………………………………………… 491
Appendix D: The Genetic Code ………………………………………… 493
Appendix E: Acronyms…………………………………………………. 495
Index ……………………………………………………………………. 507

……………………………………………………………………………………………………………………………………………………………………………………………………………………

 

Medifit  Courses Demo Certificate 

48 hours delivery

| International acceptance | Medical based | Job oriented | Lifetime validity | Most economical |

 

555 INR Demo Certificate – 2 months duration

Demo Certificate – 6 months duration

48 hours delivery after fees payment

48 hours delivery after fees payment

 

Medifit 48 hours Delivery

  Get your Certificates delivered by online mode in 48 hours after Fees payment. We try to deliver certificates in 24 hours, but the committed delivery hours are 48. Its,

Pay Today &
get Tomorrow

procedure, only by Medifit.

LIFETIME VALIDITY

Medifit issues Lifetime validity certificates for all Online Courses provided. No need to renew the certificates every 2 or 3 years. All Courses Certificates of Medifit are having Lifetime Validity. No need to renew these certificates every 2 or 3 years.

 

What makes the certificates of Medifit to get it recognized Internationally?

Vast number of students applying for Job in international market of Fitness through Medifits Online Courses Certificates. And most importantly, the Medical standards maintained, helps to acquire jobs internationally. This gives very strong International acceptance to Certificates of Medifit Courses.

 

ABOUT MEDIFIT ACADEMY CERTIFICATION COURSE:

Medifit Education Online Academy is an innovative, digital and engaging education platform that delivers fast track accredited courses and skills development courses instantly online, with no time limits, enabling individuals to study anywhere and anytime. We are proud to offer international standard courses that have helped our students build their careers across the globe.

HOW DO MEDIFIT ONLINE CERTIFICATE COURSES HELP?

Short term Professional Courses International Standards courses Opens Global opportunities Career defining Courses Skill Development Programmes Knowledge in short span Learn at your own pace Certification of Completion Immediate Earning Opportunities Positive Social Impact Optimistic Psychological Benefits Improved Standard of Living Study from anywhere & anytime Very Economical Fees

[/cmsms_text][/cmsms_column][/cmsms_row]