Introduction to proteins: structure, function, and motion
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| Main Authors: | , |
|---|---|
| Format: | Book |
| Language: | English |
| Published: |
Boca Raton [u.a.]
CRC Press
2011
|
| Series: | Chapman & Hall/CRC mathematical and computational biology series
|
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Item Description: | Includes bibliographical references |
| Physical Description: | XXVII, 626 S. Ill., graph. Darst. |
| ISBN: | 9781439810712 |
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MARC
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| 020 | |a 9781439810712 |c hardcover : alk. paper |9 978-1-4398-1071-2 | ||
| 035 | |a (OCoLC)711825362 | ||
| 035 | |a (DE-599)BVBBV037230381 | ||
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| 084 | |a CHE 820f |2 stub | ||
| 100 | 1 | |a Kessel, Amit |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Introduction to proteins |b structure, function, and motion |c Amit Kessel and Nir Ben-Tal |
| 264 | 1 | |a Boca Raton [u.a.] |b CRC Press |c 2011 | |
| 300 | |a XXVII, 626 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 490 | 0 | |a Chapman & Hall/CRC mathematical and computational biology series | |
| 500 | |a Includes bibliographical references | ||
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a Proteins |x Structure-activity relationships | |
| 650 | 4 | |a Physical biochemistry | |
| 650 | 4 | |a Proteins |x physiology | |
| 650 | 4 | |a Amino Acid Sequence | |
| 650 | 4 | |a Protein Conformation | |
| 650 | 0 | 7 | |a Molekülstruktur |0 (DE-588)4170383-2 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Chemische Struktur |0 (DE-588)4009857-6 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Proteine |0 (DE-588)4076388-2 |2 gnd |9 rswk-swf |
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| 700 | 1 | |a Ben-Tal, Nir |e Verfasser |4 aut | |
| 856 | 4 | 2 | |m Digitalisierung UB Regensburg |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021144069&sequence=000004&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
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Record in the Search Index
| _version_ | 1804143835768422400 |
|---|---|
| adam_text | Table
of
Contents
List of Boxes,
xvii
Preface,
xix
Acknowledgments,
xxv
Authors,
xxvii
Qiapit.r I
■
Introduction
1.1
THE IMPORTANCE OF PROTEINS IN LIVING ORGANISMS
1
1.1.1
Life, Proteins, and Mysterious Forces
1
1.1.2
The Molecular Organization of Living Organisms
2
1.1.3
Proteins Have Numerous Biological Roles
7
1.1.3.1
Catalysis of Metabolic Processes
7
1.1.3.2
Energy Transfer
20
1.1.3.3
Gene Expression
23
1.1.3.4
Transport of Solutes across Biological Membranes
24
1.1.3.5
Cellular Communication
24
1.1.3.6
Molecular Recognition
27
1.1.3.7
Defense
28
1.1.3.8
Forming Intracellular and Extracellular Structures
30
1.1.3.9
Cell/Tissue-Specific Functions
32
1.1.4
Physiological and Evolutionary Importance of Proteins
32
1.1.5
Medical, Industrial, and Social Importance of Proteins
33
1.1.5.1
Proteins as Drug Targets
33
1.1.5.2
Proteins as Toxin Targets
34
1.1.5.3
Industrial Applications of Proteins
35
1.2
STRUCTURAL COMPLEXITY AND ITS EFFECT ON
PROTEIN FUNCTION
36
VII
viii
■
Table of
Contents
1.3
NON-COVALENT
INTERACTIONS
BETWEEN ATOMS IN
BIOMOLECULES
40
1.3.1
Electrostatic Interactions
40
1.3.1.1
Introduction
40
1.3.1.2
Basic Principles
41
1.3.1.3
Hydrogen Bonds
48
1.3.1.4
Other Types of Electrostatic Interactions
53
1.3.2
van
der Waals
Interactions
54
1.3.3 Nonpolar
Interactions and the
Hydrophobie
Effect
56
1.3.4
Conclusions
58
1.4
SUMMARY
58
1.5
ORGANIZATION OF THE BOOK
59
REFERENCES
59
Смичтк
2 ■
Protein Structure
67
2.1
INTRODUCTION
67
2.1.1
Hierarchy in Protein Structure
67
2.1.2
Co-Enzymes and Prosthetic Groups
68
2.2
PRIMARY STRUCTURE
73
2.2.1
Amino
Acids andiheir Properties
73
2.2.1.1
Amino
Acid Structure
73
2.2.1.2
Configuration of
Amino
Acids
76
2.2.1.3
Side-Chain Properties
79
2.2.1
A Amino
Acid
Derivates in
Proteins
99
2.2.2
The
Peptide
Bond
100
2.3
SECONDARY STRUCTURE
103
2.3.1
α
-Helix
106
2.3.1.1
Geometry
106
2.3.1.2
Intramolecular Interactions 111
2.3.1.3
Amphipathic a-Helices
113
2.3.2
Non-a
Helices
114
2.3.2.1
310 Helix
115
2.3.2.2
π
Helix
116
2.3.2.3
Type II Poly-Proline Helix (PPII)
116
2.3.3
β
Conformation
117
2.3.4
Why Helices and Sheets?
119
Table
of Contents
■ ix
2.3.5
Reverse Turns
121
2.3.5.1 ß-Turn 122
2.3.5.2
Loops
123
2.3.6
Secondary Structure Preference of
Amino
Acids
123
2.3.6.1
α
Conformation
124
2.3.6.2
β
Conformation
126
2.4
TERTIARY STRUCTURE
127
2.4.1
Basic Properties of the Tertiary Structure
129
2.4.1.1
Structural Properties Required for Complex Function
129
2.4.1.2
Core versus Surface
130
2.4.1.3
Stabilizing Forces
131
2.4.2
Architecture of Proteins
131
2.4.2.1
Simple Folding Motifs
132
2.4.2.2
Complex Folds
139
2.4.2.3
Domains
147
2.4.2.4
Protein Classification
152
2.4.3
Evolutionary Conservation of Structure and Function
in Proteins
158
2.4.3.1
Interests of the Individual vs. Those of the Species
158
2.4.3.2
Structure Conservation: Evolutionary Mechanisms
160
2.4.3.3
Evolution of Function
162
2.4.4
Water Molecules inside Proteins
164
2.5
QUATERNARY STRUCTURE
165
2.5.1
Introduction
165
2.5.2
Characteristics
166
2.5.2.1
Dimensions and Complexity
166
2.5.2.2
Symmetry
167
2.5.2.3
Subunit
Interactions
168
2.5.3
Advantages of Quaternary Structure
169
2.5.3.1
Active Site Diversity
169
2.5.3.2
Time and Space Coupling of Metabolically
Related Processes
169
2.5.3.3
Regulation of Enzyme Activity
170
2.5.3.4
Stability
170
2.5.3.5
Formation of Large Structures
171
2.5.3.6
Enhancing Protein Translation Efficiency
171
χ
■
Table of Contents
2.6
POST-TRANSLATIONAL MODIFICATIONS
171
2.6.1
Introduction
171
2.6.2
Phosphorylation
172
2.6.3
Glycosylation
175
2.6.4
Acylation
178
2.6.4.1
e-N-Acetylation
178
2.6.4.2
N -Myristoylation and S-Palmitoylation
178
2.6.4.3
Ubiquitinylation
179
2.6.5
Alkylation
180
2.6.5.1
Methylation
180
2.6.5.2
S-Prenylation
181
2.6.5.3
Adenylation
181
2.6.6
Hydroxylation and Oxidation
181
2.6.7
Proteolysis
182
2.6.8
Amidation
182
2.6.9
Addition of Metal Ions
182
2.6.9.1
Stabilization of Protein Structure
183
2.6.9.2
Ligand Binding
183
2.6.9.3
Electron Transport
184
2.6.9.4
Substrate/Co-enzyme Stabilization and/or Activation
184
2.6.10
Mixed Modifications
185
2.6.11
Pathological Aspects of Post-Translational Modifications
187
2.6.11.1
Cancer
187
2.6.11.2
Age-Related Illnesses
189
2.6.12
Identifying Post-Translational Modifications
189
2.7
SUMMARY
190
REFERENCES
191
Chvì hrì
■
Methods of Structure Determination and Prediction
_________209
3.1
INTRODUCTION
209
3.2
DIFFRACTION/SCATTERING METHODS
210
3.2.1
X-ray Diffraction
210
3.2.1.1
Principles
210
3.2.1.2
Working Steps
212
3.2.1.3
Information Obtained from Crystallography
214
3.2.1.4
Problems of the Method
215
Table
of Contents
■ xi
3.2.2
Neutron Scattering
216
3.2.2.1
Principles
216
3.2.2.2
Advantages and Shortcomings
219
3.2.3
Electron Microscopy (EM)
219
3.2.3.1
Principles
219
3.2.3.2
General Steps
221
3.2.3.3
Advantages and Shortcomings
221
3.3
SPECTROSCOPIC METHODS
222
3.3.1
Nuclear Magnetic Resonance (NMR) Spectroscopy
222
3.3.1.1
Principles
222
3.3.1.2
Steps in Protein Structure Determination by Nuclear
Magnetic Resonance (NMR) Spectroscopy
225
3.3.1.3
Advantages and Shortcomings
226
3.3.2
Electron Paramagnetic Resonance (EPR) Spectroscopy
227
3.3.3
Information Derived from Other Methods
229
3.3.3.1
Fluorescent Spectroscopy
229
3.3.3.2
Circular Dichroism (CD) Spectroscopy
229
3.4
COMPUTATIONAL METHODS FOR STRUCTURE PREDICTION
230
3.4.1
Introduction
230
3.4.2
Physical Approach
230
3.4.2.1
Calculating the Total Potential Energy of the System
231
3.4.2.2
Sampling the Configurational Space of the System
236
3.4.2.3
Limitations and Partial Solutions
239
3.4.3
Comparative Approach: Homology Modeling
243
3.4.3.1
Principles
243
3.4.3.2
Principal Steps
244
3.4.3.3
Shortcoming and Overall Efficiency
246
3.4.4
Prediction, Assessment and Verification
247
3.5
CONCLUSIONS
248
3.6
PROTEIN DATA BANK (PDB)
249
3.7
SUMMARY
251
REFERENCES
253
CmpTER
4 ■
Energetics and Protein
Stability
___________________________263
4.1
BASIC PRINCIPLES OF THERMODYNAMICS
263
4.1.1
Introduction
263
xii ■
Table of Contents
4.1.2
Free Energy and Spontaneous Processes
264
4.1.3
Enthalpy, Entropy, and Molecular Thermodynamics
266
4.1.3.1
Enthalpy
266
4.1.3.2
Entropy
271
4.1.3.3
Computational Approaches Focus on Individual
Interactions
272
4.1.4
Thermodynamics and Protein Structure
274
4.2
PROTEIN STABILITY AND THE FORCES INVOLVED
274
4.2.1
How Stable Are Proteins?
274
4.2.2
Dominant Driving Forces
275
4.2.2.1
Non-polar Interactions
(AGnp)
276
4.2.2.2
Configuration Entropy Effect
(-ГДЅиЈ
278
4.2.3
Electrostatic Interactions (AGelec)
279
4.2.4
van
der Waals
Interactions (AGvdw)
283
4.2.5
Summary and Conclusions
284
4.3
PROTEIN DENATURATION AND ADAPTATION
TO EXTREME CONDITIONS
285
4.3.1
Denaturation as an Experimental Tool
285
4.3.1.1
Temperature-Dependent Denaturation
286
4.3.1.2
pH-Dependent Denaturation
286
4.3.1.3
Pressure-Induced Denaturation
287
4.3.1.4
Chemical Denaturation
287
4.3.2
Adaptation of
Proteinsto
Extreme Environments
288
4.3.2.1
Conclusions
290
4.4
STABILITY ENHANCEMENT OF INDUSTRIAL ENZYMES USING
PROTEIN ENGINEERING
290
4.4.1
Enzymes in the Industry
290
4.4.2
Enzyme Engineering
291
4.4.3
Rational Engineering of Enzymes for Increased Stability
292
4.5
SUMMARY
294
REFERENCES
296
Ch VPÍFR
5
Protein Siruciural Dynamics
303
5.1
INTRODUCTION
303
5.2
PROTEIN FOLDING
306
5.2.1
Kinetic Aspects
306
Table
of Contents
■
xüi
5.2.1.1
Levinthaľs
Paradox and the Energy Landscape Theory
306
5.2.1.2
Folding Models and Mechanisms
314
5.2.2
Folding in vivo
318
5.2.2.1
In vivo Factors That Complicate Folding
318
5.2.2.2
Assisted Folding
320
5.3
FOLDED STATE DYNAMICS
321
5.3.1
Spontaneous Dynamics
325
5.3.1.1
Proteins Are Conformational Ensembles
325
5.3.1.2
Statistical-Thermodynamic View of Protein Dynamics
326
5.3.1.3
Dynamics of Disordered Proteins
327
5.3.1.4
Biological Significance of Thermally Induced
Conformational Changes
328
5.3.1.5
Effects of the Solvent on Protein Dynamics
331
5.3.2
External Effects on Protein Dynamics
332
5.3.2.1
Ligand-Induced Dynamics and Allostery
332
5.3.2.2
Dynamics Induced by Environmental Changes
349
5.3.2.3
Enzyme-Mediated Protein Dynamics
350
5.4
METHODS FOR STUDYING PROTEIN DYNAMICS
351
5.4.1
Tools for Studying Slow (ms-sec) to Intermediary
(пѕ-цѕ)
Motions
352
5.4.2
Tools for Studying Fast Motions (fs-ps)
353
5.5
SUMMARY
354
REFERENCES
355
Chapter
6 ■
Non-Globular Proteins
________________________________367
6.1
INTRODUCTION
367
6.2
FIBROUS PROTEINS
367
6.2.1
Fiber-Based Structures Inside and Outside Cells
367
6.2.1.1
Mechanical Support
368
6.2.1.2
Tissue Organization and Cell-Environment
Communication
376
6.2.1.3
Motion
377
6.2.1.4
External Structures
379
6.2.1.5
Other Roles
379
6.2.2
Fiber-Forming vs. Fibrous Proteins
381
6.2.3
Structural Differences Between Globular and Fibrous Proteins
381
xiv ■
Table
of Contents
6.2.4
Structure-Function Relationship in the Helical Proteins
α
-Keratin
and Collagen
382
6.2.4.1
α
-Keratin
383
6.2.4.2
Collagen
385
6.3
INTRINSICALLY UNSTRUCTURED PROTEINS
392
6.3.1
Introduction
392
6.3.1.1
Molecular Recognition
394
6.3.1.2
Entropie
Chain Activity
397
6.3.2
Sequence and Structural Organization oflUPs and IDRs
398
6.3.3
Structure-Function Relationship
399
6.3.3.1
IUP Binding to Target Protein
399
6.3.3.2
Entropy Assistance-Related Roles
404
6.3.4
IUPs in vivo
405
6.4
SUMMARY
405
REFERENCES
407
Сплртгк
7 ■
Membrane Proteins
______________________________________415
7.1
INTRODUCTION
415
7.2
STRUCTURE AND ORGANIZATION OF BIOLOGICAL
MEMBRANES
418
7.2.1
General Structure and Properties
418
7.2.2
Composition of the
Lipid Bilayer
420
7.2.2.1
Glycero-Phospholipids
420
7.2.2.2
Sphingolipids
421
7.2.2.3
Sterols
422
7.2.2.4
Ethers
423
7.2.2.5
Variability
423
7.2.3
Effects of
Lipid
Properties on Those of the
Lipid
Bilayer
425
7.2.3.1
Amphipathicity
425
7.2.3.2
Asymmetry
425
7.2.3.3
Degree of Order and Thickness
426
7.2.3.4
Curvature
428
7.3
PRINCIPLES OF MEMBRANE PROTEIN STRUCTURE
430
7.3.1
Overview
430
7.3.2
Structure of Integral Membrane Proteins
431
7.3.2.1
Primary Structure
432
Table
of Contents
■ xv
7.3.2.2
Secondary Structure
438
7.3.2.3
Tertiary Structure
440
7.3.3
Peripheral Membrane Proteins
448
7.4
PROTEIN-MEMBRANE INTERACTIONS
450
7.4.1
Lipid
Bilayer Effects on Membrane Proteins
450
7.4.1.1
Effects of General Bilayer Properties
450
7.4.1.2
Effects of Specific Bilayer Lipids
454
7.4.2
Membrane Protein Effects on
Lipid
Bilayer Properties
460
7.4.2.1
Decrease in Mobility
460
7.4.2.2
Deformation and Curvature Changes
460
7.5
STRUCTURE-FUNCTION RELATIONSHIP IN MEMBRANE
PROTEINS AND PEPTIDES
463
7.5.1
Anti-Microbial Peptides
463
7.5.1.1
What Are AMPs?
463
7.5.1.2
AMP Classes
464
7.5.1.3
AMP Mechanisms of Action
466
7.5.1.4
Determinants of Activity, Selectivity, and
Toxicity
468
7.5.1.5
Other Mechanisms
471
7.5.1.6
Anti-Tumor Activity of AMPs
471
7.5.1.7
Bacterial Resistance to AMPs
473
7.5.2
G-Protein Coupled Receptors
474
7.5.2.1
Introduction
474
7.5.2.2
GPCR Signaling
475
7.5.2.3
Structure of GPCRs
476
7.5.2.4
GPCR and G-protein Activation
489
7.5.2.5
GPCR Desensitization
493
7.5.2.6
Conclusions
493
7.6
SUMMARY
495
REFERENCES
496
Protein-Liaand interactions
3Î3
8.1
INTRODUCTION
515
8.2
THEORIES ON PROTEIN-LIGAND BINDING
517
8.3
PROTEIN-LIGAND BINDING ENERGETICS
519
8.3.1
Total Binding Free Energy
519
8.3.1.1
Protein-Ligand Binding Displays Diverse Affinities
519
xvi ■
Table
of Contents
8.3.1.2
Calculating the Absolute Binding Free Energy
521
8.3.1.3
Calculating Relative Binding Energies
523
8.3.2
Thermodynamic Determinants of the Binding Energy
524
8.4
THE LIGAND-BINDING SITE
527
8.4.1
Geometric Complementarity
527
8.4.2
Electrostatic Complementarity
528
8.4.3
Binding Promiscuity
536
8.5
PROTEIN-PROTEIN INTERACTIONS
537
8.5.1
Overview
537
8.5.2
Protein-Protein Binding Domains
538
8.5.3
Structure-Function Relationships
539
8.5.3.1
Protein-Protein Interface
539
8.5.3.2
PPII Helices in Protein-Protein Interactions
547
8.6
PROTEIN-LIGAND INTERACTIONS IN DRUG ACTION
AND DESIGN
548
8.6.1
Involvement of Proteins in Disease
548
8.6.2
How Drugs Work
550
8.6.2.1
Principal Modes of Action
550
8.6.2.2
Selectivity and Side-Effects
554
8.6.3
Drug Development and Design
554
8.6.3.1
General Sources of Pharmaceutical Drugs
554
8.6.3.2
Drug Development Process
555
8.6.3.3
Principal Steps in Rational Drug Design
557
8.6.3.4
Rational Drug Design Case Study: ACE Inhibitors
567
8.7
SUMMARY
578
REFERENCES
580
ÍNDEX.
593
|
| any_adam_object | 1 |
| author | Kessel, Amit Ben-Tal, Nir |
| author_facet | Kessel, Amit Ben-Tal, Nir |
| author_role | aut aut |
| author_sort | Kessel, Amit |
| author_variant | a k ak n b t nbt |
| building | Verbundindex |
| bvnumber | BV037230381 |
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| callnumber-search | QP551 |
| callnumber-sort | QP 3551 |
| callnumber-subject | QP - Physiology |
| classification_rvk | VK 8560 WD 5100 |
| classification_tum | CHE 820f |
| ctrlnum | (OCoLC)711825362 (DE-599)BVBBV037230381 |
| dewey-full | 572/.6 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
| dewey-raw | 572/.6 |
| dewey-search | 572/.6 |
| dewey-sort | 3572 16 |
| dewey-tens | 570 - Biology |
| discipline | Chemie / Pharmazie Biologie Chemie |
| format | Book |
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| id | DE-604.BV037230381 |
| illustrated | Illustrated |
| indexdate | 2024-07-09T22:53:59Z |
| institution | BVB |
| isbn | 9781439810712 |
| language | English |
| lccn | 2010028909 |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-021144069 |
| oclc_num | 711825362 |
| open_access_boolean | |
| owner | DE-M49 DE-BY-TUM DE-355 DE-BY-UBR DE-11 DE-29T DE-19 DE-BY-UBM DE-91G DE-BY-TUM DE-20 DE-188 |
| owner_facet | DE-M49 DE-BY-TUM DE-355 DE-BY-UBR DE-11 DE-29T DE-19 DE-BY-UBM DE-91G DE-BY-TUM DE-20 DE-188 |
| physical | XXVII, 626 S. Ill., graph. Darst. |
| publishDate | 2011 |
| publishDateSearch | 2011 |
| publishDateSort | 2011 |
| publisher | CRC Press |
| record_format | marc |
| series2 | Chapman & Hall/CRC mathematical and computational biology series |
| spelling | Kessel, Amit Verfasser aut Introduction to proteins structure, function, and motion Amit Kessel and Nir Ben-Tal Boca Raton [u.a.] CRC Press 2011 XXVII, 626 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Chapman & Hall/CRC mathematical and computational biology series Includes bibliographical references Proteins Proteins Structure-activity relationships Physical biochemistry Proteins physiology Amino Acid Sequence Protein Conformation Molekülstruktur (DE-588)4170383-2 gnd rswk-swf Chemische Struktur (DE-588)4009857-6 gnd rswk-swf Proteine (DE-588)4076388-2 gnd rswk-swf Proteine (DE-588)4076388-2 s Molekülstruktur (DE-588)4170383-2 s DE-604 Chemische Struktur (DE-588)4009857-6 s b DE-604 Ben-Tal, Nir Verfasser aut Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021144069&sequence=000004&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Kessel, Amit Ben-Tal, Nir Introduction to proteins structure, function, and motion Proteins Proteins Structure-activity relationships Physical biochemistry Proteins physiology Amino Acid Sequence Protein Conformation Molekülstruktur (DE-588)4170383-2 gnd Chemische Struktur (DE-588)4009857-6 gnd Proteine (DE-588)4076388-2 gnd |
| subject_GND | (DE-588)4170383-2 (DE-588)4009857-6 (DE-588)4076388-2 |
| title | Introduction to proteins structure, function, and motion |
| title_auth | Introduction to proteins structure, function, and motion |
| title_exact_search | Introduction to proteins structure, function, and motion |
| title_full | Introduction to proteins structure, function, and motion Amit Kessel and Nir Ben-Tal |
| title_fullStr | Introduction to proteins structure, function, and motion Amit Kessel and Nir Ben-Tal |
| title_full_unstemmed | Introduction to proteins structure, function, and motion Amit Kessel and Nir Ben-Tal |
| title_short | Introduction to proteins |
| title_sort | introduction to proteins structure function and motion |
| title_sub | structure, function, and motion |
| topic | Proteins Proteins Structure-activity relationships Physical biochemistry Proteins physiology Amino Acid Sequence Protein Conformation Molekülstruktur (DE-588)4170383-2 gnd Chemische Struktur (DE-588)4009857-6 gnd Proteine (DE-588)4076388-2 gnd |
| topic_facet | Proteins Proteins Structure-activity relationships Physical biochemistry Proteins physiology Amino Acid Sequence Protein Conformation Molekülstruktur Chemische Struktur Proteine |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021144069&sequence=000004&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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