The Resource Protein folding protocols, edited by Yawen Bai and Ruth Nussinov
Protein folding protocols, edited by Yawen Bai and Ruth Nussinov
Resource Information
The item Protein folding protocols, edited by Yawen Bai and Ruth Nussinov represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in University of Missouri Libraries.This item is available to borrow from 1 library branch.
Resource Information
The item Protein folding protocols, edited by Yawen Bai and Ruth Nussinov represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in University of Missouri Libraries.
This item is available to borrow from 1 library branch.
- Summary
- Protein Folding Protocols presents protocols for studying and characterizing protein folding from the unfolded to the folded state. Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences. These approaches have tremendous implications, ranging from drug design, functional assignment, comprehension of the nature of regulation, understanding molecular machines, viral entry into cells, and putting together cellular pathways and their dynamics
- Language
- eng
- Extent
- 1 online resource (xiii, 327 pages)
- Contents
-
- Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins / F. Gai, D. Du and Y. Xu
- The use of high-pressure nuclear magnetic resonance to study protein folding / M.W. Lassalle and K. Akasaka
- Characterization of denatured proteins using residual dipolar couplings / E.B. Gebel and D. Shortle
- Characterizing residual structure in disordered protein States using nuclear magnetic resonance / D. Eliezer
- Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance / Y. Bai, H. Feng and Z. Zhou
- Characterizing protein folding transition States using Psi-analysis / A.D. Pandit [and others]
- Advances in the analysis of conformational transitions in peptides using differential scanning calorimetry / W.W. Streicher and G.I. Makhatadze
- Application of single molecule Forster resonance energy transfer to protein folding / B. Schuler
- Single molecule studies of protein folding using atomic force microscopy / S.P. Ng, L.G. Randles and J. Clarke
- Using triplet-triplet energy transfer to measure conformational dynamics in polypeptide chains / B. Fierz [and others]
- A hierarchical protein folding scheme based on the building block folding model / N. Haspel [and others]
- Replica exchange molecular dynamics method for protein folding simulation / R. Zhou
- Estimation of folding probabilities and phi values from molecular dynamics simulations of reversible Peptide folding / F. Rao, G. Settanni and A. Caflisch
- Packing regularities in biological structures relate to their dynamics / R.L. Jernigan and A. Kloczkowski
- Intermediates and transition states in protein folding / D. Thirumalai and D.K. Klimov
- Thinking the impossible: how to solve the protein folding problem with and without homologous structures and more / R. Casadio [and others]
- Isbn
- 9781280832581
- Label
- Protein folding protocols
- Title
- Protein folding protocols
- Statement of responsibility
- edited by Yawen Bai and Ruth Nussinov
- Language
- eng
- Summary
- Protein Folding Protocols presents protocols for studying and characterizing protein folding from the unfolded to the folded state. Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences. These approaches have tremendous implications, ranging from drug design, functional assignment, comprehension of the nature of regulation, understanding molecular machines, viral entry into cells, and putting together cellular pathways and their dynamics
- Cataloging source
- COO
- Dewey number
- 572/.633
- Illustrations
- illustrations
- Index
- index present
- LC call number
- QP551
- LC item number
- .P695822 2007
- Literary form
- non fiction
- NAL call number
- QH506
- NAL item number
- .M45 v. 350
- Nature of contents
-
- dictionaries
- bibliography
- NLM call number
-
- W1
- QU 55
- NLM item number
-
- ME9616J v.350 2007
- P96635 2007
- http://library.link/vocab/relatedWorkOrContributorName
-
- Bai, Yawen
- Nussinov, Ruth
- Series statement
- Methods in molecular biology,
- Series volume
- 350
- http://library.link/vocab/subjectName
-
- Protein folding
- Proteins
- Proteins
- Protein Folding
- Protein Conformation
- Proteins
- SCIENCE
- Protein folding
- Proteins
- Proteins
- Label
- Protein folding protocols, edited by Yawen Bai and Ruth Nussinov
- Bibliography note
- Includes bibliographical references and index
- Carrier category
- online resource
- Carrier category code
-
- cr
- Carrier MARC source
- rdacarrier
- Content category
- text
- Content type code
-
- txt
- Content type MARC source
- rdacontent
- Contents
- Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins / F. Gai, D. Du and Y. Xu -- The use of high-pressure nuclear magnetic resonance to study protein folding / M.W. Lassalle and K. Akasaka -- Characterization of denatured proteins using residual dipolar couplings / E.B. Gebel and D. Shortle -- Characterizing residual structure in disordered protein States using nuclear magnetic resonance / D. Eliezer -- Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance / Y. Bai, H. Feng and Z. Zhou -- Characterizing protein folding transition States using Psi-analysis / A.D. Pandit [and others] -- Advances in the analysis of conformational transitions in peptides using differential scanning calorimetry / W.W. Streicher and G.I. Makhatadze -- Application of single molecule Forster resonance energy transfer to protein folding / B. Schuler -- Single molecule studies of protein folding using atomic force microscopy / S.P. Ng, L.G. Randles and J. Clarke -- Using triplet-triplet energy transfer to measure conformational dynamics in polypeptide chains / B. Fierz [and others] -- A hierarchical protein folding scheme based on the building block folding model / N. Haspel [and others] -- Replica exchange molecular dynamics method for protein folding simulation / R. Zhou -- Estimation of folding probabilities and phi values from molecular dynamics simulations of reversible Peptide folding / F. Rao, G. Settanni and A. Caflisch -- Packing regularities in biological structures relate to their dynamics / R.L. Jernigan and A. Kloczkowski -- Intermediates and transition states in protein folding / D. Thirumalai and D.K. Klimov -- Thinking the impossible: how to solve the protein folding problem with and without homologous structures and more / R. Casadio [and others]
- Control code
- 262691302
- Dimensions
- unknown
- Extent
- 1 online resource (xiii, 327 pages)
- Form of item
- online
- Isbn
- 9781280832581
- Media category
- computer
- Media MARC source
- rdamedia
- Media type code
-
- c
- Other physical details
- illustrations.
- http://library.link/vocab/ext/overdrive/overdriveId
- 978-1-58829-622-1
- Specific material designation
- remote
- System control number
- (OCoLC)262691302
- Label
- Protein folding protocols, edited by Yawen Bai and Ruth Nussinov
- Bibliography note
- Includes bibliographical references and index
- Carrier category
- online resource
- Carrier category code
-
- cr
- Carrier MARC source
- rdacarrier
- Content category
- text
- Content type code
-
- txt
- Content type MARC source
- rdacontent
- Contents
- Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins / F. Gai, D. Du and Y. Xu -- The use of high-pressure nuclear magnetic resonance to study protein folding / M.W. Lassalle and K. Akasaka -- Characterization of denatured proteins using residual dipolar couplings / E.B. Gebel and D. Shortle -- Characterizing residual structure in disordered protein States using nuclear magnetic resonance / D. Eliezer -- Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance / Y. Bai, H. Feng and Z. Zhou -- Characterizing protein folding transition States using Psi-analysis / A.D. Pandit [and others] -- Advances in the analysis of conformational transitions in peptides using differential scanning calorimetry / W.W. Streicher and G.I. Makhatadze -- Application of single molecule Forster resonance energy transfer to protein folding / B. Schuler -- Single molecule studies of protein folding using atomic force microscopy / S.P. Ng, L.G. Randles and J. Clarke -- Using triplet-triplet energy transfer to measure conformational dynamics in polypeptide chains / B. Fierz [and others] -- A hierarchical protein folding scheme based on the building block folding model / N. Haspel [and others] -- Replica exchange molecular dynamics method for protein folding simulation / R. Zhou -- Estimation of folding probabilities and phi values from molecular dynamics simulations of reversible Peptide folding / F. Rao, G. Settanni and A. Caflisch -- Packing regularities in biological structures relate to their dynamics / R.L. Jernigan and A. Kloczkowski -- Intermediates and transition states in protein folding / D. Thirumalai and D.K. Klimov -- Thinking the impossible: how to solve the protein folding problem with and without homologous structures and more / R. Casadio [and others]
- Control code
- 262691302
- Dimensions
- unknown
- Extent
- 1 online resource (xiii, 327 pages)
- Form of item
- online
- Isbn
- 9781280832581
- Media category
- computer
- Media MARC source
- rdamedia
- Media type code
-
- c
- Other physical details
- illustrations.
- http://library.link/vocab/ext/overdrive/overdriveId
- 978-1-58829-622-1
- Specific material designation
- remote
- System control number
- (OCoLC)262691302
Subject
- Protein Conformation
- Protein Folding
- Protein folding
- Protein folding
- Protein folding
- Proteins -- Analysis
- Proteins -- Analysis
- Proteins -- Analysis
- Proteins -- Conformation
- Proteins -- Conformation
- Proteins -- Conformation
- Proteins -- analysis
- SCIENCE -- Life Sciences | Biochemistry
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<div class="citation" vocab="http://schema.org/"><i class="fa fa-external-link-square fa-fw"></i> Data from <span resource="http://link.library.missouri.edu/portal/Protein-folding-protocols-edited-by-Yawen-Bai/1MzGRTx98hg/" typeof="Book http://bibfra.me/vocab/lite/Item"><span property="name http://bibfra.me/vocab/lite/label"><a href="http://link.library.missouri.edu/portal/Protein-folding-protocols-edited-by-Yawen-Bai/1MzGRTx98hg/">Protein folding protocols, edited by Yawen Bai and Ruth Nussinov</a></span> - <span property="potentialAction" typeOf="OrganizeAction"><span property="agent" typeof="LibrarySystem http://library.link/vocab/LibrarySystem" resource="http://link.library.missouri.edu/"><span property="name http://bibfra.me/vocab/lite/label"><a property="url" href="http://link.library.missouri.edu/">University of Missouri Libraries</a></span></span></span></span></div>
