國立虎尾科技大學 |

Protein folding

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Protein folding / Grace E. Orellana and Ellinor Haglund, authors.
作者:	Orellana, Grace E.,
其他作者:	Haglund, Ellinor,
面頁冊數:	1 online resource :illustrations (some color). :
標題:	Biotechnology industries. -
電子資源:	https://dx.doi.org/10.1021/acsinfocus.7e7032
ISBN:	9780841296381

Protein folding
Orellana, Grace E.,

Protein folding [electronic resource] /Grace E. Orellana and Ellinor Haglund, authors. - 1 online resource :illustrations (some color). - ACS in focus,2691-8307. - ACS in focus,.

Includes bibliographical references and index.

Protein Folding --

"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."--

ISBN: 9780841296381

Standard No.: 10.1021/acsinfocus.7e7032doiSubjects--Topical Terms:

654278
Biotechnology industries.
Index Terms--Genre/Form:

554714
Electronic books.

LC Class. No.: QP551 / .O746 2024eb

Dewey Class. No.: 574.19/245

National Library of Medicine Call No.: QU 55 / O746 2024

Protein folding
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245 1 0 $a Protein folding $c Grace E. Orellana and Ellinor Haglund, authors. $h [electronic resource] /
264 1 $a Washington, DC, USA : $b American Chemical Society, $c 2024.
300 $a 1 online resource : $b illustrations (some color).
336 $a text $2 rdacontent
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490 1 $a ACS in focus, $x 2691-8307
504 $a Includes bibliographical references and index.
505 0 0 $t Protein Folding -- $t Biophysical Characterization of Proteins.
520 3 $a "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."-- $c Provided by publisher.
590 $a American Chemical Society, Protein Folding eBooks - 2024 Front Files.
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650 # 0 $a Amino acid sequence. $3 812790
650 # 0 $a Polypeptides. $3 796708
650 # 0 $a Cellulase $x Structure. $3 1483762
650 # 0 $a Aggregation (Chemistry) $3 681960
650 # 0 $a Aggregation (Chemistry) $x Mechanism of action $x Testing. $3 1483763
650 # 0 $a Proteins $x Formation. $3 1483764
650 # 0 $a Molecular chaperones. $3 882817
650 # 0 $a Proteins $x Physiological transport. $3 668385
650 # 0 $a Endoplasmic reticulum. $3 669092
650 # 0 $a Insulin-like growth factor-binding proteins. $3 1483765
650 # 0 $a Eukaryotic cells. $3 883434
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650 # 0 $a Molecular chaperones $x Utilization. $3 1483767
650 # 0 $a Ribonucleases $x Experiments. $3 1483768
650 # 0 $a Micelles $x Utilization. $3 1483769
650 # 0 $a Liposomes $x Utilization. $3 1483770
650 # 0 $a Amino acids $x Structure $x Experiments. $3 1483771
650 # 0 $a Escherichia coli $x Biotechnology. $3 1483772
650 # 0 $a Filgrastim $x Synthesis $x Methodology. $3 1483773
650 # 0 $a Immunoglobulins $x Biotechnology. $3 787693
650 # 0 $a Monoclonal antibodies $x Biotechnology. $3 1483774
650 # 0 $a Somatotropin $x Spectra. $3 1483775
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650 1 2 $a Cellulase $x chemistry. $3 1483776
650 1 2 $a Chemical Precipitation. $3 1483777
650 1 2 $a Proteins. $3 584006
650 1 2 $a Molecular Chaperones. $3 1238586
650 1 2 $a Proteins $x pharmacokinetics. $3 778500
650 1 2 $a Endoplasmic Reticulum. $3 1483778
650 1 2 $a Eukaryotic Cells. $3 654973
650 1 2 $a Models, Theoretical. $3 528501
650 1 2 $a Ribonucleases. $3 786115
650 1 2 $a Micelles. $3 1065644
650 1 2 $a Liposomes. $3 583574
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650 1 2 $a Escherichia coli. $3 895584
650 1 2 $a Filgrastim $x chemical synthesis. $3 1483780
650 1 2 $a Immunoglobulins. $3 676923
650 1 2 $a Antibodies, Monoclonal. $3 1177543
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