1.

Record Nr.

UNINA9910713503203321

Autore

Dinger Eric C.

Titolo

Integrated aquatic community and water quality monitoring of mountain ponds and lakes in the Klamath Network / / Eric C. Dinger [and three others]

Pubbl/distr/stampa

Fort Collins, Colorado : , : U.S. Department of the Interior, National Park Service, Natural Resource Stewardship and Science, , 2012

Descrizione fisica

1 online resource (xvi, 234 pages) : color illustrations, color maps

Collana

Natural resource report ; ; NPS/KLMN/NRR--2012/484

Soggetti

Aquatic ecology - Klamath National Forest (Calif. and Or.)

Ecological surveys - Klamath National Forest (Calif. and Or.)

Water quality - Klamath National Forest (Calif. and Or.) - Measurement

Ponds - Klamath National Forest (Calif. and Or.)

Lakes - Klamath National Forest (Calif. and Or.)

Environmental monitoring - Klamath National Forest (Calif. and Or.)

Klamath National Forest (Calif. and Or.)

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

"NPS 963/112291, January 2012"--Page ii.

"Experience your America"--Page 254.

Includes tables.

Nota di bibliografia

Includes bibliographical references.



2.

Record Nr.

UNINA9911020074103321

Autore

Kinter Michael

Titolo

Protein sequencing and identification using tandem mass spectrometry / / Michael Kinter, Nicholas E. Sherman

Pubbl/distr/stampa

New York, : Wiley-Interscience, c2000

ISBN

9786610541669

9781280541667

1280541660

9780471231882

0471231886

9780471721987

0471721980

Descrizione fisica

1 online resource (321 p.)

Collana

Wiley-Interscience series on mass spectrometry

Altri autori (Persone)

ShermanNicholas E

Disciplina

572.8/5

Soggetti

Nucleotide sequence

Proteins

Mass spectrometry

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.

Nota di bibliografia

Includes bibliographical references and index.

Nota di contenuto

PROTEIN SEQUENCING AND IDENTIFICATION USING TANDEM MASS SPECTROMETRY; CONTENTS; Series Preface; Preface; Chapter 1. An Introduction to Protein Sequencing Using Tandem Mass Spectrometry; 1.1. Introduction; 1.2. References; Chapter 2. The Primary Structure of Proteins and a Historical Overview of Protein Sequencing; 2.1. Protein and Peptide Structure; 2.2. Edman Degradation; 2.2.1. The Edman Reaction; 2.2.2. Incorporation of the Edman Degradation Reaction into Automated Protein Sequenators; 2.2.3. Edman Degradation in Proteomic Research; 2.3. Tandem Mass Spectrometry

2.3.1. A Brief History of the Application of Mass Spectrometry to Protein Sequencing2.3.2. Sequence Analysis of Peptides Using Electron Ionization Mass Spectrometry; 2.3.3. The Utilization of Fast Atom Bombardment with Tandem Mass Spectrometry to Sequence Peptides; 2.3.4. Internal Sequence Analysis of Proteins Using Electrospray Ionization-Tandem Mass Spectrometry and Matrix-Assisted Laser



Desorption/Ionization-Time-of- Flight Mass Spectrometry; 2.4. Summary; 2.5. References; Chapter 3. Fundamental Mass Spectrometry; 3.1. An Overview of the Instrumentation; 3.2. Ionization Methods

3.2.1. Electrospray Ionization3.2.2. Nanospray and Microspray Ionization; 3.2.3. Matrix-Assisted Laser Desorption/ Ionization; 3.3. Mass Analyzers; 3.3.1. Fundamental Parameters of Mass Analysis; 3.3.2. Quadrupole Mass Filters (3.20); 3.3.3. Ion Trap Mass Analyzers (3.21-3.23); 3.3.4. Time-of-Flight Mass Analyzers (3.5); 3.4. Tandem Mass Spectrometry; 3.4.1. Collisionally Induced Dissociation; 3.4.2. Tandem Mass Spectrometers; 3.4.3. Types of Tandem Mass Spectrometry Experiments; 3.5. Data Systems; 3.6. Summary; 3.7. References

Chapter 4. Collisionally Induced Dissociation of Protonated Peptide Ions and the Interpretation of Product Ion Spectra4.1. Introduction; 4.2. Peptide Fragmentation Chemistry; 4.2.1. Collisionally Induced Dissociation of Peptide Ions Formed by Electrospray Ionization; 4.2.2. Fragmentation of Protonated Peptide Ions Formed by Matrix-Assisted Laser Desorption/Ionization; 4.3. Interpretation of the Product Ion Spectra of Tryptic Peptides; 4.3.1. Tabulated Values Used in the Interpretation; 4.3.2. A Strategy for the Interpretation of Product Ion Spectra of Tryptic Peptides

4.3.3. Sample Interpretation Problem Number One4.3.4. Sample Interpretation Problem Number Two; 4.3.5. A Summary of Interpretation Problems One and Two; 4.3.6. Examples of More Difficult Product Ion Spectra That Cannot Be Completely Interpreted; 4.3.7. Interpretation of Product Ion Spectra from Triply Charged Ions; 4.4. Summary; 4.5. References; Chapter 5. Basic Polyacrylamide Gel Electrophoresis; 5.1. Introduction; 5.2. The Principles of Gel Electrophoresis; 5.2.1. Protein Movement and Separation; 5.2.2. Protein Detection

5.3. The Basic Steps in a Polyacrylamide Gel Electrophoresis Experiment

Sommario/riassunto

How to design, execute, and interpret experiments for protein sequencing using mass spectrometry The rapid expansion of searchable protein and DNA databases in recent years has triggered an explosive growth in the application of mass spectrometry to protein sequencing. This timely and authoritative book provides professionals and scientists in biotechnology research with complete coverage of procedures for analyzing protein sequences by mass spectrometry, including step-by-step guidelines for sample preparation, analysis, and data interpretation. Michael Kinter and Nicholas Sherman