Structural biology of membrane proteins:
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Cambridge
RSC Publ.
2006
|
| Schriftenreihe: | RSC biomolecular sciences
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XXIII, 392 S. Ill. 24 cm |
| ISBN: | 0854043616 9780854043613 |
Internformat
MARC
| LEADER | 00000nam a2200000 c 4500 | ||
|---|---|---|---|
| 001 | BV021602083 | ||
| 003 | DE-604 | ||
| 005 | 20060823 | ||
| 007 | t | ||
| 008 | 060531s2006 a||| |||| 00||| eng d | ||
| 020 | |a 0854043616 |9 0-85404-361-6 | ||
| 020 | |a 9780854043613 |9 978-0-85404-361-3 | ||
| 035 | |a (OCoLC)255014905 | ||
| 035 | |a (DE-599)BVBBV021602083 | ||
| 040 | |a DE-604 |b ger |e aacr | ||
| 041 | 0 | |a eng | |
| 049 | |a DE-M49 |a DE-703 |a DE-355 |a DE-526 | ||
| 050 | 0 | |a QP552.M44 | |
| 082 | 0 | |a 572.696 | |
| 084 | |a WE 5000 |0 (DE-625)148296: |2 rvk | ||
| 084 | |a CHE 887f |2 stub | ||
| 084 | |a CHE 806f |2 stub | ||
| 084 | |a CHE 820f |2 stub | ||
| 245 | 1 | 0 | |a Structural biology of membrane proteins |c ed. by Reinhard Grisshammer ... |
| 264 | 1 | |a Cambridge |b RSC Publ. |c 2006 | |
| 300 | |a XXIII, 392 S. |b Ill. |c 24 cm | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 490 | 0 | |a RSC biomolecular sciences | |
| 650 | 4 | |a Membrane proteins | |
| 650 | 0 | 7 | |a Membranproteine |0 (DE-588)4130026-9 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Strukturchemie |0 (DE-588)4183790-3 |2 gnd |9 rswk-swf |
| 655 | 7 | |0 (DE-588)4143413-4 |a Aufsatzsammlung |2 gnd-content | |
| 655 | 4 | |a Aufsatzsammlung - Membranproteine - Molekülstruktur | |
| 689 | 0 | 0 | |a Membranproteine |0 (DE-588)4130026-9 |D s |
| 689 | 0 | 1 | |a Strukturchemie |0 (DE-588)4183790-3 |D s |
| 689 | 0 | |5 DE-604 | |
| 700 | 1 | |a Grisshammer, Reinhard |e Sonstige |4 oth | |
| 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=014817409&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-014817409 | ||
Datensatz im Suchindex
| _version_ | 1804135384905416704 |
|---|---|
| adam_text | Contents
Section
Chapter I Refolding of G-Protein-Coupled Receptors
Jean-Louis Banères
1
2
3
4
4.1
4.2
4.3
4.4
5
References
Chapter
Membrane Proteins in Mammalian Cells
Philip J. Reeves
1
2
3
Mammalian Cells
3.1
3.2
3.2.1
of HEK293S Cells
3.3
3.4
4
Expression of Eukaryotic Membrane Proteins
4.1
4.2
xji
4.3
Expression
4.3.1
HEK293S Stable
Inducible
5
Purification
5.1
Culture Using a Bioreactor
5.2
of Rhodopsin
6
Containing Simple N-Glycans
7
Tetracycline-Inducible Cell Lines
for Large-Scale Preparation of
Other Eukaryotic Membrane Proteins
References
Chapter
Receptors for Structural Biology
Filippo Mancia
1
1.1
Coupled Receptors
1.2
ofGPCRs
1.3
2
2.1
2.2
Functional GPCRs
2.3
Mammalian Cells
2.4
Transfection or Viral Infection of
Mammalian Cells
2.5
2.6
2.7
2.8
Contents
3
Acknowledgments
References
Chapter
Receptors for Crystallization
Tony Warne
1
1.1
Coupled Receptors
1.2
Receptor
2
2.1
Post-Translational Modifications
2.1.1
2.1.2
2.1.3
2.2
3
and Detergent Selection
3.1
3.2
Crystallization
4
4.1
4.2
4.3
4.4
and Assembly of Complexes
4.5
5
Aggregational State,
6
Acknowledgments
References
Chapter
Use in Membrane Protein Studies
Fabien
I Introduction
Contents
2
Protein Studies
2.1
Detergents
2.1.1
2.1.2
2.1.3
2.1.4
2.1.5
2.2
2.3
3
Common Detergents
3.1
3.2
Presence of Detergents
3.2.1
3.2.2
4
Crystallization
4.1
4.2
Lipid
4.3
4.4
Membrane Proteins
4.4.1
Membrane Protein from
Vibrio Cholerae
4.4.2
Monomeric Outer Membrane
Phospholipase A
4.5
Membrane Protein Contact
4.5.1
4.5.2
Trigonal Crystal Form
4.6
Interactions in Crystals
5
Acknowledgements
References
Contents xv
Section
Membrane Proteins
Chapter
Structure and Dynamics of Integral
Membrane Proteins
John H. Bushweller,
Yunpeng Zhou
1
2
NMR Studies
2.1
2.2
3
Membrane Proteins
3.1
Strategies Using TROSY-Based Experiments
3.2
the Limit of Sensitivity
3.3
Number of Nuclear Overhauser Effect-Derived
Distance Constraints
3.4
for Long Range Distances
3.5
4
Membrane Proteins
4.1
4.2
4.3
5
Membrane Proteins
5.1
5.2
5.3
6
Protein Dynamics
6.1
6.2
7
References
Chapter
Solid-State NMR
Adam
1
2
2.1
Sample Preparation
2.2
Determination
3
3.1
3.2
3.3
4
Acknowledgements
References
Chapter
Assessing Structure and Dynamics of Native
Membrane Proteins
W. Kukulski, T.
D. Fotiadis and A.
Abstract
1
2
3
3.1
3.2
3.3
3.4
4
4.1
4.2
4.3
4.4
4.5
4.6
Chapter
5
References
State-of-the-Art Methods in Electron
Microscopy, including Single-Particle Analysis
VinzenzM.
1
Contents
118
118
118
118
120
121
121
121
124
125
126
126
131
131
131
132
135
135
138
138
139
142
142
143
143
144
144
145
147
147
152
152
Contenti
2 Sample
3
3.1 Sample
3.2 Radiation
4
4.1
4.1.1
4.1.2
4.1.3
4.1.4
4.2
4.2.1
of Crystalline Samples over
Single Particles
4.2.2
Straightening
4.2.3
crystals and CTF-Correction
4.2.4
Calculation of
5
5.1
5.2
6
References
Chapter
Membrane Proteins Using Cubic
Crystallization
Hartmut Luecke
1
1.1
Techniques
1.2
1.3
1.3.1
1.3.2
1.4
Crystallization
1.5
Crystallization
1.6
2
xviii
2.1
Membrane Proteins
2.2
Method
2.3
2.4
3
at High Resolution
4
References
Section
Chapter
Channel Proteins
Robert M. Stroud, William E.C. Harries, John Lee,
Shahram Khademi and David Savage
1
2
Aquaporins
2.1
NPA Motif
2.2
2.3
3
4
Glycerol
4.1
5
their Functional Implications
5.1
Aquaporin
5.2
Organization
5.3
Acknowledgment
References
Chapter
Shahram Khademi and Robert M. Stroud
1
2
Contents xjx
2.1 Overall
of
2.2
Twofold Symmetry
2.3
3
as a Channel that Conducts NH3
4
4.1
4.2
4.3
5
6
7
Acknowledgment
References
Chapter
of Mycobacter
Georg E.
1
2
2.1
2.2
2.3
3
3.1
3.2 ß-Barrels 242
3.3
4
4.1
4.2
5
Acknowledgments
References
Chapter
Translocation Channel
Bert Van Den Berg and Ian Collinson
1
1.1
1.2
Chapter
Chapter
Contents
2
Electron Cryo-Microscopy
3
SecY Complex
4
5
5.1
Translocation
6
References
Structure and Function of the Translocator
Domain of Bacterial
Peter Van Ulsen,
Jan Tommassen
1
2
3
4
Translocator Domain
5
6
to Other Translocator Domains and to TolC
7
References
Х
of Sarcoplasmic Reticulum Ca2+-ATPase
at the Atomic Level
Jesper
Lykke
1
2
of Ca2+ Transport
3
4
5
Calcium Ion Occlusion
6
Transport
7
8
Contents xxj
9
References
Chapter
EmrE Structures Determined by
Electron Cryomicroscopy and X-ray
Crystallography
CG.
1
2
3
4
Cryomicroscopy
5
by Electron Crystallography with a
Resolution Structure Determined by X-ray
Crystallography
6
References
Chapter
Raimund Fromme, Ingo Grotjohann
Petra Fromme
1
320
2 Photosystem
324
2.1
324
2.2
325
2.2.1
(PsbA and PsbD)
325
2.2.2
CP43 (PsbB and PsbC)
325
2.2.3
325
2.2.4
Subunits
327
2.2.5
and PsbU
327
2.3
Photosystem
327
2.3.1
Transport Chain in
328
2.3.2
Transfer Chain of
329
xxii Contents
2.4
3 Photosystem
3.1
3.2
3.2.1
Subunits PsaA and PsaB
3.2.2
Photosystem
3.2.3
PsaD, and PsaE
3.3
Photosystem
339
3.3.1
P700: The Primary Electron Donor
340
3.3.2
A: The Initial Electron Acceptor
340
3.3.3
Ao: The First Stable Electron Acceptor
341
3.3.4
A,: The Phylloquinone
341
3.3.5
Fx: The First FeS Cluster
342
3.3.6
FA and FB: The Terminal FeS Clusters
342
3.4
342
3.4.1
The Chlorophylls
343
3.4.2
The Carotenoids
343
3.4.3
The Lipids in
344
4
and Outlook
344
References
344
Chapter
Structural Insights into Molecular
Mechanisms
Avinash Gill and Dean R. Madden
1
Introduction
349
1.1
Physiological and Pathophysiological
Roles of the Ionotropic
350
1.2
Medicinal Chemistry
351
1.3
Ionotropic
Modular
351
Studies of the Ligand-Binding Domain
351
2.1
Overall Structure
353
2.2
Pharmacological Specificity
353
2.3
Ligand-Binding Domain Conformational
Changes
354
2.4
Correlation with Channel Activation
355
2.5
Dimerization
356
Contents
2.6 Desensitization
Dimer Interface
3
Receptor Ion Channel
3.1
Glutamate
3.2
Subunit Assembly
3.3
Domains
4
4.1
and Gating
4.2
5
5.1
5.2
5.3
5.4
References
Chapter
Eva Pebay-Pey
1
2
3
4
5
6
6.1
6.2
6.3
7
Acknowledgments
References
Subject Index
|
| adam_txt |
Contents
Section
Chapter I Refolding of G-Protein-Coupled Receptors
Jean-Louis Banères
1
2
3
4
4.1
4.2
4.3
4.4
5
References
Chapter
Membrane Proteins in Mammalian Cells
Philip J. Reeves
1
2
3
Mammalian Cells
3.1
3.2
3.2.1
of HEK293S Cells
3.3
3.4
4
Expression of Eukaryotic Membrane Proteins
4.1
4.2
xji
4.3
Expression
4.3.1
HEK293S Stable
Inducible
5
Purification
5.1
Culture Using a Bioreactor
5.2
of Rhodopsin
6
Containing Simple N-Glycans
7
Tetracycline-Inducible Cell Lines
for Large-Scale Preparation of
Other Eukaryotic Membrane Proteins
References
Chapter
Receptors for Structural Biology
Filippo Mancia
1
1.1
Coupled Receptors
1.2
ofGPCRs
1.3
2
2.1
2.2
Functional GPCRs
2.3
Mammalian Cells
2.4
Transfection or Viral Infection of
Mammalian Cells
2.5
2.6
2.7
2.8
Contents
3
Acknowledgments
References
Chapter
Receptors for Crystallization
Tony Warne
1
1.1
Coupled Receptors
1.2
Receptor
2
2.1
Post-Translational Modifications
2.1.1
2.1.2
2.1.3
2.2
3
and Detergent Selection
3.1
3.2
Crystallization
4
4.1
4.2
4.3
4.4
and Assembly of Complexes
4.5
5
Aggregational State,
6
Acknowledgments
References
Chapter
Use in Membrane Protein Studies
Fabien
I Introduction
Contents
2
Protein Studies
2.1
Detergents
2.1.1
2.1.2
2.1.3
2.1.4
2.1.5
2.2
2.3
3
Common Detergents
3.1
3.2
Presence of Detergents
3.2.1
3.2.2
4
Crystallization
4.1
4.2
Lipid
4.3
4.4
Membrane Proteins
4.4.1
Membrane Protein from
Vibrio Cholerae
4.4.2
Monomeric Outer Membrane
Phospholipase A
4.5
Membrane Protein Contact
4.5.1
4.5.2
Trigonal Crystal Form
4.6
Interactions in Crystals
5
Acknowledgements
References
Contents xv
Section
Membrane Proteins
Chapter
Structure and Dynamics of Integral
Membrane Proteins
John H. Bushweller,
Yunpeng Zhou
1
2
NMR Studies
2.1
2.2
3
Membrane Proteins
3.1
Strategies Using TROSY-Based Experiments
3.2
the Limit of Sensitivity
3.3
Number of Nuclear Overhauser Effect-Derived
Distance Constraints
3.4
for Long Range Distances
3.5
4
Membrane Proteins
4.1
4.2
4.3
5
Membrane Proteins
5.1
5.2
5.3
6
Protein Dynamics
6.1
6.2
7
References
Chapter
Solid-State NMR
Adam
1
2
2.1
Sample Preparation
2.2
Determination
3
3.1
3.2
3.3
4
Acknowledgements
References
Chapter
Assessing Structure and Dynamics of Native
Membrane Proteins
W. Kukulski, T.
D. Fotiadis and A.
Abstract
1
2
3
3.1
3.2
3.3
3.4
4
4.1
4.2
4.3
4.4
4.5
4.6
Chapter
5
References
State-of-the-Art Methods in Electron
Microscopy, including Single-Particle Analysis
VinzenzM.
1
Contents
118
118
118
118
120
121
121
121
124
125
126
126
131
131
131
132
135
135
138
138
139
142
142
143
143
144
144
145
147
147
152
152
Contenti
2 Sample
3
3.1 Sample
3.2 Radiation
4
4.1
4.1.1
4.1.2
4.1.3
4.1.4
4.2
4.2.1
of Crystalline Samples over
Single Particles
4.2.2
Straightening
4.2.3
crystals and CTF-Correction
4.2.4
Calculation of
5
5.1
5.2
6
References
Chapter
Membrane Proteins Using Cubic
Crystallization
Hartmut Luecke
1
1.1
Techniques
1.2
1.3
1.3.1
1.3.2
1.4
Crystallization
1.5
Crystallization
1.6
2
xviii
2.1
Membrane Proteins
2.2
Method
2.3
2.4
3
at High Resolution
4
References
Section
Chapter
Channel Proteins
Robert M. Stroud, William E.C. Harries, John Lee,
Shahram Khademi and David Savage
1
2
Aquaporins
2.1
NPA Motif
2.2
2.3
3
4
Glycerol
4.1
5
their Functional Implications
5.1
Aquaporin
5.2
Organization
5.3
Acknowledgment
References
Chapter
Shahram Khademi and Robert M. Stroud
1
2
Contents xjx
2.1 Overall
of
2.2
Twofold Symmetry
2.3
3
as a Channel that Conducts NH3
4
4.1
4.2
4.3
5
6
7
Acknowledgment
References
Chapter
of Mycobacter
Georg E.
1
2
2.1
2.2
2.3
3
3.1
3.2 ß-Barrels 242
3.3
4
4.1
4.2
5
Acknowledgments
References
Chapter
Translocation Channel
Bert Van Den Berg and Ian Collinson
1
1.1
1.2
Chapter
Chapter
Contents
2
Electron Cryo-Microscopy
3
SecY Complex
4
5
5.1
Translocation
6
References
Structure and Function of the Translocator
Domain of Bacterial
Peter Van Ulsen,
Jan Tommassen
1
2
3
4
Translocator Domain
5
6
to Other Translocator Domains and to TolC
7
References
Х
of Sarcoplasmic Reticulum Ca2+-ATPase
at the Atomic Level
Jesper
Lykke
1
2
of Ca2+ Transport
3
4
5
Calcium Ion Occlusion
6
Transport
7
8
Contents xxj
9
References
Chapter
EmrE Structures Determined by
Electron Cryomicroscopy and X-ray
Crystallography
CG.
1
2
3
4
Cryomicroscopy
5
by Electron Crystallography with a
Resolution Structure Determined by X-ray
Crystallography
6
References
Chapter
Raimund Fromme, Ingo Grotjohann
Petra Fromme
1
320
2 Photosystem
324
2.1
324
2.2
325
2.2.1
(PsbA and PsbD)
325
2.2.2
CP43 (PsbB and PsbC)
325
2.2.3
325
2.2.4
Subunits
327
2.2.5
and PsbU
327
2.3
Photosystem
327
2.3.1
Transport Chain in
328
2.3.2
Transfer Chain of
329
xxii Contents
2.4
3 Photosystem
3.1
3.2
3.2.1
Subunits PsaA and PsaB
3.2.2
Photosystem
3.2.3
PsaD, and PsaE
3.3
Photosystem
339
3.3.1
P700: The Primary Electron Donor
340
3.3.2
A: The Initial Electron Acceptor
340
3.3.3
Ao: The First Stable Electron Acceptor
341
3.3.4
A,: The Phylloquinone
341
3.3.5
Fx: The First FeS Cluster
342
3.3.6
FA and FB: The Terminal FeS Clusters
342
3.4
342
3.4.1
The Chlorophylls
343
3.4.2
The Carotenoids
343
3.4.3
The Lipids in
344
4
and Outlook
344
References
344
Chapter
Structural Insights into Molecular
Mechanisms
Avinash Gill and Dean R. Madden
1
Introduction
349
1.1
Physiological and Pathophysiological
Roles of the Ionotropic
350
1.2
Medicinal Chemistry
351
1.3
Ionotropic
Modular
351
Studies of the Ligand-Binding Domain
351
2.1
Overall Structure
353
2.2
Pharmacological Specificity
353
2.3
Ligand-Binding Domain Conformational
Changes
354
2.4
Correlation with Channel Activation
355
2.5
Dimerization
356
Contents
2.6 Desensitization
Dimer Interface
3
Receptor Ion Channel
3.1
Glutamate
3.2
Subunit Assembly
3.3
Domains
4
4.1
and Gating
4.2
5
5.1
5.2
5.3
5.4
References
Chapter
Eva Pebay-Pey
1
2
3
4
5
6
6.1
6.2
6.3
7
Acknowledgments
References
Subject Index |
| any_adam_object | 1 |
| any_adam_object_boolean | 1 |
| building | Verbundindex |
| bvnumber | BV021602083 |
| callnumber-first | Q - Science |
| callnumber-label | QP552 |
| callnumber-raw | QP552.M44 |
| callnumber-search | QP552.M44 |
| callnumber-sort | QP 3552 M44 |
| callnumber-subject | QP - Physiology |
| classification_rvk | WE 5000 |
| classification_tum | CHE 887f CHE 806f CHE 820f |
| ctrlnum | (OCoLC)255014905 (DE-599)BVBBV021602083 |
| dewey-full | 572.696 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
| dewey-raw | 572.696 |
| dewey-search | 572.696 |
| dewey-sort | 3572.696 |
| dewey-tens | 570 - Biology |
| discipline | Biologie Chemie |
| discipline_str_mv | Biologie Chemie |
| format | Book |
| fullrecord | <?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01716nam a2200457 c 4500</leader><controlfield tag="001">BV021602083</controlfield><controlfield tag="003">DE-604</controlfield><controlfield tag="005">20060823 </controlfield><controlfield tag="007">t</controlfield><controlfield tag="008">060531s2006 a||| |||| 00||| eng d</controlfield><datafield tag="020" ind1=" " ind2=" "><subfield code="a">0854043616</subfield><subfield code="9">0-85404-361-6</subfield></datafield><datafield tag="020" ind1=" " ind2=" "><subfield code="a">9780854043613</subfield><subfield code="9">978-0-85404-361-3</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(OCoLC)255014905</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)BVBBV021602083</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-604</subfield><subfield code="b">ger</subfield><subfield code="e">aacr</subfield></datafield><datafield tag="041" ind1="0" ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="049" ind1=" " ind2=" "><subfield code="a">DE-M49</subfield><subfield code="a">DE-703</subfield><subfield code="a">DE-355</subfield><subfield code="a">DE-526</subfield></datafield><datafield tag="050" ind1=" " ind2="0"><subfield code="a">QP552.M44</subfield></datafield><datafield tag="082" ind1="0" ind2=" "><subfield code="a">572.696</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">WE 5000</subfield><subfield code="0">(DE-625)148296:</subfield><subfield code="2">rvk</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">CHE 887f</subfield><subfield code="2">stub</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">CHE 806f</subfield><subfield code="2">stub</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">CHE 820f</subfield><subfield code="2">stub</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural biology of membrane proteins</subfield><subfield code="c">ed. by Reinhard Grisshammer ...</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Cambridge</subfield><subfield code="b">RSC Publ.</subfield><subfield code="c">2006</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">XXIII, 392 S.</subfield><subfield code="b">Ill.</subfield><subfield code="c">24 cm</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="490" ind1="0" ind2=" "><subfield code="a">RSC biomolecular sciences</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Membrane proteins</subfield></datafield><datafield tag="650" ind1="0" ind2="7"><subfield code="a">Membranproteine</subfield><subfield code="0">(DE-588)4130026-9</subfield><subfield code="2">gnd</subfield><subfield code="9">rswk-swf</subfield></datafield><datafield tag="650" ind1="0" ind2="7"><subfield code="a">Strukturchemie</subfield><subfield code="0">(DE-588)4183790-3</subfield><subfield code="2">gnd</subfield><subfield code="9">rswk-swf</subfield></datafield><datafield tag="655" ind1=" " ind2="7"><subfield code="0">(DE-588)4143413-4</subfield><subfield code="a">Aufsatzsammlung</subfield><subfield code="2">gnd-content</subfield></datafield><datafield tag="655" ind1=" " ind2="4"><subfield code="a">Aufsatzsammlung - Membranproteine - Molekülstruktur</subfield></datafield><datafield tag="689" ind1="0" ind2="0"><subfield code="a">Membranproteine</subfield><subfield code="0">(DE-588)4130026-9</subfield><subfield code="D">s</subfield></datafield><datafield tag="689" ind1="0" ind2="1"><subfield code="a">Strukturchemie</subfield><subfield code="0">(DE-588)4183790-3</subfield><subfield code="D">s</subfield></datafield><datafield tag="689" ind1="0" ind2=" "><subfield code="5">DE-604</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Grisshammer, Reinhard</subfield><subfield code="e">Sonstige</subfield><subfield code="4">oth</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="m">Digitalisierung UB Regensburg</subfield><subfield code="q">application/pdf</subfield><subfield code="u">http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=014817409&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA</subfield><subfield code="3">Inhaltsverzeichnis</subfield></datafield><datafield tag="999" ind1=" " ind2=" "><subfield code="a">oai:aleph.bib-bvb.de:BVB01-014817409</subfield></datafield></record></collection> |
| genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content Aufsatzsammlung - Membranproteine - Molekülstruktur |
| genre_facet | Aufsatzsammlung Aufsatzsammlung - Membranproteine - Molekülstruktur |
| id | DE-604.BV021602083 |
| illustrated | Illustrated |
| index_date | 2024-07-02T14:48:03Z |
| indexdate | 2024-07-09T20:39:39Z |
| institution | BVB |
| isbn | 0854043616 9780854043613 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-014817409 |
| oclc_num | 255014905 |
| open_access_boolean | |
| owner | DE-M49 DE-BY-TUM DE-703 DE-355 DE-BY-UBR DE-526 |
| owner_facet | DE-M49 DE-BY-TUM DE-703 DE-355 DE-BY-UBR DE-526 |
| physical | XXIII, 392 S. Ill. 24 cm |
| publishDate | 2006 |
| publishDateSearch | 2006 |
| publishDateSort | 2006 |
| publisher | RSC Publ. |
| record_format | marc |
| series2 | RSC biomolecular sciences |
| spelling | Structural biology of membrane proteins ed. by Reinhard Grisshammer ... Cambridge RSC Publ. 2006 XXIII, 392 S. Ill. 24 cm txt rdacontent n rdamedia nc rdacarrier RSC biomolecular sciences Membrane proteins Membranproteine (DE-588)4130026-9 gnd rswk-swf Strukturchemie (DE-588)4183790-3 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Aufsatzsammlung - Membranproteine - Molekülstruktur Membranproteine (DE-588)4130026-9 s Strukturchemie (DE-588)4183790-3 s DE-604 Grisshammer, Reinhard Sonstige oth Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=014817409&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Structural biology of membrane proteins Membrane proteins Membranproteine (DE-588)4130026-9 gnd Strukturchemie (DE-588)4183790-3 gnd |
| subject_GND | (DE-588)4130026-9 (DE-588)4183790-3 (DE-588)4143413-4 |
| title | Structural biology of membrane proteins |
| title_auth | Structural biology of membrane proteins |
| title_exact_search | Structural biology of membrane proteins |
| title_exact_search_txtP | Structural biology of membrane proteins |
| title_full | Structural biology of membrane proteins ed. by Reinhard Grisshammer ... |
| title_fullStr | Structural biology of membrane proteins ed. by Reinhard Grisshammer ... |
| title_full_unstemmed | Structural biology of membrane proteins ed. by Reinhard Grisshammer ... |
| title_short | Structural biology of membrane proteins |
| title_sort | structural biology of membrane proteins |
| topic | Membrane proteins Membranproteine (DE-588)4130026-9 gnd Strukturchemie (DE-588)4183790-3 gnd |
| topic_facet | Membrane proteins Membranproteine Strukturchemie Aufsatzsammlung Aufsatzsammlung - Membranproteine - Molekülstruktur |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=014817409&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT grisshammerreinhard structuralbiologyofmembraneproteins |