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Protein folding / Grace E. Orellana and Ellinor Haglund, authors.
Author
Orellana, Grace E.
[Browse]
Format
Book
Language
English
Published/Created
Washington, DC, USA : American Chemical Society, 2024.
Description
1 online resource : illustrations (some color).
Details
Subject(s)
Biotechnology industries
[Browse]
Amino acid sequence
[Browse]
Polypeptides
[Browse]
Cellulase
—
Structure
[Browse]
Aggregation (Chemistry)
[Browse]
Aggregation (Chemistry)
—
Mechanism of action
—
Testing
[Browse]
Proteins
—
Formation
[Browse]
Molecular chaperones
[Browse]
Proteins
—
Physiological transport
[Browse]
Endoplasmic reticulum
[Browse]
Insulin-like growth factor-binding proteins
[Browse]
Eukaryotic cells
[Browse]
Protein folding
—
Mathematical models
[Browse]
Molecular chaperones
—
Utilization
[Browse]
Ribonucleases
—
Experiments
[Browse]
Micelles
—
Utilization
[Browse]
Liposomes
—
Utilization
[Browse]
Amino acids
—
Structure
—
Experiments
[Browse]
Escherichia coli
—
Biotechnology
[Browse]
Filgrastim
—
Synthesis
—
Methodology
[Browse]
Immunoglobulins
—
Biotechnology
[Browse]
Monoclonal antibodies
—
Biotechnology
[Browse]
Somatotropin
—
Spectra
[Browse]
Author
Haglund, Ellinor
[Browse]
Related name
American Chemical Society
[Browse]
Series
ACS in focus,
[More in this series]
ACS in focus, 2691-8307
[More in this series]
Summary note
"Life as we know it would not exist if proteins did not fold into functional three-dimensional structures, where α-helices, loops, and β-sheets act together to form active sites that drive a myriad of biochemical reactions in the cell. The failure of this process is linked to the pathology of various diseases, such as neurodegenerative disorders like Alzheimer's, genetic conditions (like cystic fibrosis), and cancer. It is no wonder that close to $2 billion in worldwide research funding has been devoted over the last five years (2019-2025) to helping scientists understand the molecular details of protein folding, how it can fail in ways that promote disease in humans, and clinical paths to treat or prevent diseases linked to protein misfolding. This primer is prerequisite reading to the literature on this important topic for readers new to the field. Chapter one provides exposure to the three-dimensional structure of proteins -- readers will learn how to identify secondary structures, protein motifs, and domains involved in biological function. Chapter two introduces methodologies to determine the three-dimensional structure of proteins -- readers will learn modern techniques to determine the secondary structure composition and the orientation of atoms in three-dimensional space. By providing exposure to how the physical environment (i.e., chemical denaturants, pH, pressure, and temperature) controls protein denaturation, readers will learn how such information can be used to study the biophysical characteristics of proteins through various probes and methodologies."-- Provided by publisher.
Notes
American Chemical Society, Protein Folding eBooks - 2024 Front Files.
Bibliographic references
Includes bibliographical references and index.
Contents
Protein Folding
Biophysical Characterization of Proteins.
ISBN
9780841296381 (electronic)
Doi
10.1021/acsinfocus.7e7032
Statement on language in description
Princeton University Library aims to describe library materials in a manner that is respectful to the individuals and communities who create, use, and are represented in the collections we manage.
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