The BAM complex : methods and protocols / edited by Susan K. Buchanan, Nicholas Noinaj.
This volume is comprised of a collection of experimental protocols for common techniques and strategies used to study the biogenesis of b-barrel outer membrane proteins in Gram-negative bacteria. The book guides readers through methods on the function of the BAM complex, the roles played by each of...
Saved in:
| Online Access: |
Full Text (via Springer) |
|---|---|
| Other Authors: | , |
| Format: | Electronic eBook |
| Language: | English |
| Published: |
New York :
Humana Press : Springer,
[2015]
|
| Series: | Methods in molecular biology (Clifton, N.J.) ;
v. 1329. |
| Subjects: |
MARC
| LEADER | 00000cam a2200000 i 4500 | ||
|---|---|---|---|
| 001 | in00000138972 | ||
| 006 | m o d | ||
| 007 | cr ||||||||||| | ||
| 008 | 151104t20152015nyua ob 001 0 eng d | ||
| 005 | 20240605205123.6 | ||
| 015 | |a GBB8J9217 |2 bnb | ||
| 016 | 7 | |a 101674608 |2 DNLM | |
| 016 | 7 | |a 019098003 |2 Uk | |
| 019 | |a 964873004 |a 967613446 |a 1005769272 | ||
| 020 | |a 9781493928712 |q (eBook) | ||
| 020 | |a 1493928716 |q (eBook) | ||
| 020 | |z 9781493928705 |q (Trade Cloth) | ||
| 020 | |z 1493928708 |q (Trade Cloth) | ||
| 020 | |a 1493928708 | ||
| 020 | |a 9781493928705 | ||
| 024 | 3 | |a 9781493928705 | |
| 029 | 1 | |a AU@ |b 000061151136 | |
| 029 | 1 | |a UKMGB |b 019098003 | |
| 035 | |a (OCoLC)spr927449821 | ||
| 035 | |a (OCoLC)927449821 |z (OCoLC)964873004 |z (OCoLC)967613446 |z (OCoLC)1005769272 | ||
| 037 | |a spr978-1-4939-2871-2 | ||
| 040 | |a RML |b eng |e rda |e pn |c RML |d RML |d OCLCO |d YDXCP |d SCB |d OCLCQ |d COO |d AZU |d OCLCO |d OCLCF |d OCLCQ |d OCLCO |d GW5XE |d BUF |d VT2 |d OCL |d CAUOI |d OCLCO |d OCLCA |d LVT |d OCLCO |d OCLCA |d UAB |d OCLCO |d OTZ |d TFH |d OCLCO |d OCLCA |d OCLCQ |d CASUM |d MERER |d OCLCQ |d U3W |d OCLCO |d UKMGB |d OCLCO |d OCLCA |d OCLCQ |d OCLCO |d OCLCQ |d OCLCA |d NLW |d OCLCO |d OCLCQ |d OCL |d OCLCO |d OCLCA |d OCLCL |d OCLCQ | ||
| 049 | |a GWRE | ||
| 050 | 4 | |a QP552.M44 | |
| 050 | 4 | |a QD431-431.7QH601-602 | |
| 060 | 4 | |a W1 |b ME9616J v.1329 2015 | |
| 060 | 4 | |a QW 25 | |
| 066 | |c (S | ||
| 245 | 0 | 4 | |a The BAM complex : |b methods and protocols / |c edited by Susan K. Buchanan, Nicholas Noinaj. |
| 264 | 1 | |a New York : |b Humana Press : |b Springer, |c [2015] | |
| 264 | 4 | |c ©2015 | |
| 300 | |a 1 online resource (xi, 283 pages) : |b illustrations (some color) | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 490 | 1 | |a Methods in molecular medicine ; |v 1329 | |
| 504 | |a Includes bibliographical references and index. | ||
| 520 | 8 | |a This volume is comprised of a collection of experimental protocols for common techniques and strategies used to study the biogenesis of b-barrel outer membrane proteins in Gram-negative bacteria. The book guides readers through methods on the function of the BAM complex, the roles played by each of the individual components, the expression and purification of the components, crystallization and structure determination of the components, and how the individual Bam components may assemble into a functional complex. | |
| 505 | 0 | 0 | |t The [beta]-barrel assembly machinery complex / |r Denise L. Leyton, Matthew J. Belousoff, and Trevor Lithgow -- |t Yeast mitochondria as a model system to study the biogenesis of bacterial [beta]-barrel proteins / |r Thomas Ulrich [and three others] -- |t Experimental methods for studying the BAM complex in Neisseria meningitides / |r Martine P. Bos, Ria Tommassen-van Boxtel, and Jan Tommassen -- |t Heart modifiability of outer membrane proteins from gram-negative bacteria / |r Nicholas Noinaj, Adam J. Kuszak, and Susan K. Buchanan -- |t The role of a destabilized membrane of OMP insertion / |r Ashlee M. Plummer, Dennis Gessmann, and Karen G. Fleming -- |t Treponema pallidum in gel microdroplets: a method for topological analysis of BamA (TP0326) and localization of rare outer membrane proteins / |r Amit Luthra, Arvind Anand, and Justin D. Radolf -- |t Analyzing the role of periplasmic folding factors in the biogenesis of OMPs and members of the Type V secretion system / |r Gustavo Bodelón, Elvira Marín, and Luis Ángel Fernandez -- |t An in vitro assay for substrate translocation by FhaC in liposomes / |r Enguo Fan, Derrick Norell, and Matthias Müller -- |t Measuring cell-cell binding using flow-cytometry / |r Zachary C. Ruhe, Christopher S. Hayes, and David A. Low -- |t Methods to characterize folding and function of BamA cross-link mutants / |r Adam J. Kuszak, Nicholas Noinaj, and Susan K. Buchanan -- |t Small angle X-ray scattering (SAXS) characterization of the POTRA domains of BamA / |r Pamela Arden Doerner and Marcelo Carlos Sousa -- |t Assessing the outer membrane insertion and folding of multimeric transmembrane [beta]-barrel proteins / |r Jack C. Leo, Philipp Oberhettinger, and Dirk Linke -- |t The expression, purification, and structure determination of BamA from E. coli / |r Dongchun Ni and Yihua Huang -- |t Expression and purification of the individual Bam components BamB-E / |r Suraaj Aulakh, Kelly H. Kim, and Mark Paetzel -- |t Structure determination of the BAM complex accessory lipoproteins BamB-E / |r Kornelius Zeth -- |t An in vitro assay for outer membrane protein assembly by the BAM complex / |r Giselle Roman-Hernandez and Harris D. Bernstein -- |t Identification of BamC on the surface of E. coli / |r Chaille T. Webb and Trevor Lithgow -- |t Construction and characterization of an E. coli bamD depletion strain / |r Dante R. Ricci -- |t Expression, purification, and screening of BamE, a component of the BAM complex, for structural characterization / |r Mark Jeeves, Pooja Sridhar, and Timothy J. Knowles -- |t Purification and bicelle crystallization for structure determination of the E. coli outer membrane protein TamA / |r Fabian Gruss, Sebastian Hiller, and Timm Maier -- |t Strategies for the analysis of Bam recognition motifs in outer membrane proteins / |r Nagarajan Paramasivam and Dirk Linke -- |t Summary and future directions / |r Nicholas Noinaj and Susan K. Buchanan. |
| 650 | 0 | |a Membrane proteins. | |
| 650 | 0 | |a Life sciences. | |
| 650 | 0 | |a Proteins. | |
| 650 | 0 | |a Cell membranes. | |
| 650 | 0 | |a Genetics |x Technique. | |
| 650 | 7 | |a Genetics |x Technique |2 fast | |
| 650 | 7 | |a Membrane proteins |2 fast | |
| 650 | 7 | |a Cell membranes |2 fast | |
| 650 | 7 | |a Life sciences |2 fast | |
| 650 | 7 | |a Proteins |2 fast | |
| 655 | 7 | |a Laboratory manuals |2 fast | |
| 700 | 1 | |a Buchanan, Susan K., |e editor. | |
| 700 | 1 | |a Noinaj, Nicholas, |e editor. | |
| 758 | |i has work: |a The BAM complex (Text) |1 https://id.oclc.org/worldcat/entity/E39PCFBcQmMyy4Bb3k83hkD9wy |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |t Bam complex |z 9781493928705 |
| 830 | 0 | |a Methods in molecular biology (Clifton, N.J.) ; |v v. 1329. |x 1064-3745 | |
| 856 | 4 | 0 | |u https://colorado.idm.oclc.org/login?url=https://link.springer.com/10.1007/978-1-4939-2871-2 |z Full Text (via Springer) |
| 880 | 0 | 0 | |6 505-00/(S |t β-Barrel assembly machinery complex / |r Denisse L. Leyton, Matthew J. Belousoff and Trevor Lithgow -- |t Yeast mitochondria as a model system to study the biogenesis of bacterial β-barrel proteins / |r Thomas Ulrich [and others] -- |t Experimental methods for studying the BAM complex in Neisseria meningitidis / |r Martine P. Bos, Ria Tommassen-van Boxtel, and Jan Tommassen -- |t Heat modifiability of outer membrane proteins from gram-negative bacteria / |r Nicholas Noinaj, Adam J. Kuszak, and Susan K. Buchanan -- |t Role of a destabilized membrane for OMP insertion / |r Ashlee M. Plummer, Dennis Gessmann, and Karen G. Fleming -- |t Treponema pallidum in gel microdroplets : a method for topological analysis of BamA (TP0326) and localization of rare outer membrane proteins / |r Amit Luthra, Arvind Anand, and Justin D. Radolf -- |t Analyzing the role of periplasmic folding factors in the biogenesis of OMPs and members of the type V secretion system / |r Gustavo Bodelón, Elvira Marín, and Luis Ángel Fernández -- |t In vitro assay for substrate translocation by FhaC in liposomes / |r Enguo Fan, Derrick Norell, and Matthias Müller-- |t Measuring cell-cell binding using flow-cytometry / |r Zachary C. Ruhe, Christopher S. Hayes, and David A. Low -- |t Methods to characterize folding and function of BamA cross-link mutants / |r Adam J. Kuszak, Nicholas Noinaj, and Susan K. Buchanan -- |t Small angle X-ray scattering (SAXS) characterization of the POTRA domains of BamA / |r Pamela Arden Doerner and Marcelo Carlos Sousa -- |t Assessing the outer membrane insertion and folding of multimeric transmembrane β-barrel proteins / |r Jack C. Leo, Philipp Oberhettinger, and Dirk Linke -- |t Expression, purification, and structure determination of BamA from E. coli / |r Dongchun Ni and Yihua Huang -- |t Expression and purification of the individual Bam components BamB-E / |r Suraaj Aulakh, Kelly H. Kim, and Mark Paetzel -- |t Structure determination of the BAM complex accessory lipoproteins BamB-E / |r Kornelius Zeth -- |t In vitro assay for outer membrane protein assembly by the BAM complex / |r Giselle Roman-Hernandez and Harris D. Bernstein -- |t Identification of BamC on the surface of E. coli / |r Chaille T. Webb and Trevor Lithgow -- |t Construction and characterization of an E. coli bamD depletion strain / |r Dante P. Ricci -- |t Expression, purification, and screening of BamE, a component of the BAM complex, for structural characterization / |r Mark Jeeves, Pooja Sridhar, and Timothy J. Knowles -- |t Purification and bicelle crystallization for structure determination of the E. coli outer membrane protein TamA / |r Fabian Gruss, Sebastian Hiller, and Timm Maier -- |t Strategies for the analysis of Bam recognition motifs in outer membrane proteins / |r Nagarajan Paramasivam and Dirk Linke -- |t Summary and future directions / |r Nicholas Noinaj and Susan K. Buchanan. |
| 915 | |a - | ||
| 956 | |a Springer Protocols | ||
| 956 | |b Springer Nature - Complete Protocols | ||
| 994 | |a 92 |b COD | ||
| 998 | |b WorldCat record encoding level change | ||
| 999 | f | f | |s 92e677d8-ad31-4e76-bce9-2a19a9612e1d |i 210df0f7-bb8d-4048-b8e0-7b14b7af763c |
| 952 | f | f | |p Can circulate |a University of Colorado Boulder |b Online |c Online |d Online |e QP552.M44 |h Library of Congress classification |i web |