The Resource Biophysics and the Challenges of Emerging Threats, edited by Joseph Puglisi, (electronic resource)

Biophysics and the Challenges of Emerging Threats, edited by Joseph Puglisi, (electronic resource)

Label
Biophysics and the Challenges of Emerging Threats
Title
Biophysics and the Challenges of Emerging Threats
Statement of responsibility
edited by Joseph Puglisi
Title variation
Proceedings of the NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats Erice, Sicily, Italy 19-30 June 2007
Creator
Contributor
Editor
Editor
Subject
Language
eng
Summary
Single-molecule techniques eliminate ensemble averaging, thus revealing transient or rare species in heterogeneous systems [1–3]. These approaches have been employed to probe myriad biological phenomena, including protein and RNA folding [4–6], enzyme kinetics [7, 8], and even protein biosynthesis [1, 9, 10]. In particular, immobilization-based fluorescence te- niques such as total internal reflection fluorescence microscopy (TIRF-M) have recently allowed for the observation of multiple events on the millis- onds to seconds timescale [11–13]. Single-molecule fluorescence methods are challenged by the instability of single fluorophores. The organic fluorophores commonly employed in single-molecule studies of biological systems display fast photobleaching, intensity fluctuations on the millisecond timescale (blinking), or both. These phenomena limit observation time and complicate the interpretation of fl- rescence fluctuations [14, 15]. Molecular oxygen (O) modulates dye stability. Triplet O efficiently 2 2 quenches dye triplet states responsible for blinking. This results in the for- tion of singlet oxygen [16–18]. Singlet O reacts efficiently with organic dyes, 2 amino acids, and nucleobases [19, 20]. Oxidized dyes are no longer fluor- cent; oxidative damage impairs the folding and function of biomolecules. In the presence of saturating dissolved O , blinking of fluorescent dyes is sup- 2 pressed, but oxidative damage to dyes and biomolecules is rapid. Enzymatic O -scavenging systems are commonly employed to ameliorate dye instability. 2 Small molecules are often employed to suppress blinking at low O levels
Member of
Is Subseries of
Dewey number
571.4
http://bibfra.me/vocab/relation/httpidlocgovvocabularyrelatorsedt
-5Bgrv124H0
LC call number
QH301-705
Literary form
non fiction
http://bibfra.me/vocab/lite/meetingDate
2007
http://bibfra.me/vocab/lite/meetingName
NATO Advanced Study Institute on Biophysics and the Challenges of Emerging Threats
Nature of contents
dictionaries
http://library.link/vocab/relatedWorkOrContributorName
Puglisi, Joseph.
Series statement
NATO Science for Peace and Security Series B: Physics and Biophysics,
http://library.link/vocab/subjectName
  • Life sciences
  • Biotechnology
  • Chemistry
  • Life Sciences, general
  • Biological and Medical Physics, Biophysics
  • Biotechnology
  • Solid State Physics
  • Spectroscopy and Microscopy
  • Theoretical and Computational Chemistry
Label
Biophysics and the Challenges of Emerging Threats, edited by Joseph Puglisi, (electronic resource)
Instantiates
Publication
Note
Selected conference papers
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
A Simple Model for Protein Folding -- Complementarity of Hydrophobic/Hydrophilic Properties In Protein—Ligand Complexes: A New Tool to Improve Docking Results -- Structures of Cvnh Family Lectins -- Biophysical Approaches To Study Dna Base Flipping -- The Diversity of Nuclear Magnetic Resonance Spectroscopy -- Improved Dye Stability in Single-Molecule Fluorescence Experiments -- The Evaluation of Isotope Editing and Filtering for Protein—Ligand Interaction Elucidation by Nmr -- Ribosome: an Ancient Cellular Nano-Machine for Genetic Code Translation
Dimensions
unknown
Edition
1st ed. 2009.
Extent
1 online resource (180 p.)
Form of item
online
Isbn
9781282364837
Media category
computer
Media MARC source
rdamedia
Media type code
  • c
Other control number
10.1007/978-90-481-2368-1
Specific material designation
remote
System control number
  • (CKB)1000000000754157
  • (EBL)450946
  • (OCoLC)647813283
  • (DE-He213)978-90-481-2368-1
  • (MiAaPQ)EBC450946
  • (EXLCZ)991000000000754157
Label
Biophysics and the Challenges of Emerging Threats, edited by Joseph Puglisi, (electronic resource)
Publication
Note
Selected conference papers
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
A Simple Model for Protein Folding -- Complementarity of Hydrophobic/Hydrophilic Properties In Protein—Ligand Complexes: A New Tool to Improve Docking Results -- Structures of Cvnh Family Lectins -- Biophysical Approaches To Study Dna Base Flipping -- The Diversity of Nuclear Magnetic Resonance Spectroscopy -- Improved Dye Stability in Single-Molecule Fluorescence Experiments -- The Evaluation of Isotope Editing and Filtering for Protein—Ligand Interaction Elucidation by Nmr -- Ribosome: an Ancient Cellular Nano-Machine for Genetic Code Translation
Dimensions
unknown
Edition
1st ed. 2009.
Extent
1 online resource (180 p.)
Form of item
online
Isbn
9781282364837
Media category
computer
Media MARC source
rdamedia
Media type code
  • c
Other control number
10.1007/978-90-481-2368-1
Specific material designation
remote
System control number
  • (CKB)1000000000754157
  • (EBL)450946
  • (OCoLC)647813283
  • (DE-He213)978-90-481-2368-1
  • (MiAaPQ)EBC450946
  • (EXLCZ)991000000000754157

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