date: 2013-10-07T08:16:59Z
pdf:PDFVersion: 1.5
pdf:docinfo:title: Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-?c Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy
xmp:CreatorTool: Microsoft® Office Word 2007
access_permission:can_print_degraded: true
subject: Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-?c window (defined as ?c < supra-?c < 40 ms; in which ?c is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-?c window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-?c scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-?c scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-?c scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
language: en-US
dc:format: application/pdf; version=1.5
pdf:docinfo:creator_tool: Microsoft® Office Word 2007
access_permission:fill_in_form: true
pdf:encrypted: false
dc:title: Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-?c Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy
modified: 2013-10-07T08:16:59Z
cp:subject: Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-?c window (defined as ?c < supra-?c < 40 ms; in which ?c is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-?c window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-?c scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-?c scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-?c scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
pdf:docinfo:subject: Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-?c window (defined as ?c < supra-?c < 40 ms; in which ?c is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-?c window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-?c scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-?c scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-?c scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
pdf:docinfo:creator: David Ban, T. Michael Sabo, Christian Griesinger, Donghan Lee
meta:author: David Ban, T. Michael Sabo, Christian Griesinger, Donghan Lee
meta:creation-date: 2013-10-07T16:15:15Z
created: 2013-10-07T16:15:15Z
access_permission:extract_for_accessibility: true
Creation-Date: 2013-10-07T16:15:15Z
Author: David Ban, T. Michael Sabo, Christian Griesinger, Donghan Lee
producer: Microsoft® Office Word 2007
pdf:docinfo:producer: Microsoft® Office Word 2007
pdf:unmappedUnicodeCharsPerPage: 0
dc:description: Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-?c window (defined as ?c < supra-?c < 40 ms; in which ?c is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-?c window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-?c scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-?c scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-?c scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
Keywords: supra-?c; RDC; relaxation dispersion; R1r; CPMG; protein dynamics; 
NMR spectroscopy

access_permission:modify_annotations: true
dc:creator: David Ban, T. Michael Sabo, Christian Griesinger, Donghan Lee
description: Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-?c window (defined as ?c < supra-?c < 40 ms; in which ?c is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-?c window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-?c scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-?c scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-?c scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
dcterms:created: 2013-10-07T16:15:15Z
Last-Modified: 2013-10-07T08:16:59Z
dcterms:modified: 2013-10-07T08:16:59Z
title: Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-?c Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy
xmpMM:DocumentID: uuid:1cf5f970-fdfa-454c-8bf3-84ad183cc08d
Last-Save-Date: 2013-10-07T08:16:59Z
pdf:docinfo:keywords: supra-?c; RDC; relaxation dispersion; R1r; CPMG; protein dynamics; 
NMR spectroscopy

pdf:docinfo:modified: 2013-10-07T08:16:59Z
meta:save-date: 2013-10-07T08:16:59Z
Content-Type: application/pdf
X-Parsed-By: org.apache.tika.parser.DefaultParser
creator: David Ban, T. Michael Sabo, Christian Griesinger, Donghan Lee
dc:language: en-US
dc:subject: supra-?c; RDC; relaxation dispersion; R1r; CPMG; protein dynamics; 
NMR spectroscopy

access_permission:assemble_document: true
xmpTPg:NPages: 34
pdf:charsPerPage: 2218
access_permission:extract_content: true
access_permission:can_print: true
meta:keyword: supra-?c; RDC; relaxation dispersion; R1r; CPMG; protein dynamics; 
NMR spectroscopy

access_permission:can_modify: true
pdf:docinfo:created: 2013-10-07T16:15:15Z