Proteins
A Structural Biology Perspective
- 1st Edition - November 25, 2024
- Imprint: Academic Press
- Author: Jia-huai Wang
- Language: English
- Paperback ISBN:9 7 8 - 0 - 3 2 3 - 9 9 8 9 3 - 2
- eBook ISBN:9 7 8 - 0 - 3 2 3 - 9 9 9 5 0 - 2
Proteins: A Structural Biology Perspective explains how advances in modern physics fueled the birth of structural biology and modern molecular biology in the early to mid 20th cent… Read more
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Request a sales quoteProteins: A Structural Biology Perspective explains how advances in modern physics fueled the birth of structural biology and modern molecular biology in the early to mid 20th century. Scientifically rigorous and deeply informed by the author’s own 60-year career as a structural biologist, the book provides historical and personal accounts of how two generations of renowned scientists doggedly pursued their research projects to arrive at milestone achievements, while also covering basic aspects of protein structures and their evolution with a special focus on molecules at the surface of cells and viruses. Since 1962, when only a single structure for myoglobin had been determined at atomic resolution, the rapidly evolving field has grown exponentially to fill protein structure databases (PDB) worldwide with hundred thousands of structures for basic research and medical advancement. From “What is a Wave?” to “What Is Life?”, Proteins: A Structural Biology Perspective takes readers on a uniquely intimate journey through the past 100 years of protein science, while providing an up-to-the-minute assessment of successful structure prediction by AI models like AlphaFold and RoseTTAFold and where it’s all likely to lead. Outfitted with detailed illustrations and authoritative citations, this is a valuable resource for graduate students and young research scientists in biology and the medical sciences.
- Provides readers with the knowledge and mindset necessary to explore the molecular intricacies of biological systems through the lens of protein structures
- Focuses on two points: from genomic perspective and from protein-protein interaction view of protein structures
Academic sector and maybe drug development industry sector; It can be used as a reference book for programs of biochemistry, biophysics, molecular biology, immunology, neural science and other medical sciences
- Title of Book
- Cover image
- Title page
- Table of Contents
- Copyright
- Foreword
- Acknowledgments
- 1. From “What is a wave?” to “What is life?”: the structural biology boom
- Abstract
- Body
- 1.1 What is a wave?
- 1.2 What is life?
- 1.3 Birth of structural biology and molecular biology
- 1.4 A new era in biology
- 1.5 The boom in structural biology
- 1.6 A giant leap forward—artificial intelligence in structural biology
- 1.7 The book
- References
- 2. From α to β: the beginning of protein structure analyses
- Abstract
- 2.1 The primary structure of a protein: sequencing insulin
- 2.2 The α keratin and β keratin: a pioneering achievement in structural biology
- 2.3 The discovery of the α helix: Pauling’s approach to protein structure
- 2.4 The basics of an α helix
- 2.5 Biophysical features of the α helix
- 2.6 α helix in the “leucine zipper” motif
- 2.7 The α helix in membrane proteins
- 2.8 The 310 helix and π helix
- 2.9 From β keratin to β pleated sheet
- 2.10 The basics of a β pleated sheet
- 2.11 The basic β structure motifs
- 2.12 Assembly of β structure motifs
- References
- 3. Proteins-in-modules and genes-in-pieces. How proteins evolve
- Abstract
- 3.1 Proteins are modular with functional and kinetic advantage
- 3.2 Supersecondary structure and domain classification
- 3.3 The biology of modular protein dynamics—the bilobal case
- 3.4 Multidomain modular proteins for complex biological functions
- 3.5 Functional domains are often evolutionarily conserved
- 3.6 Domain and exon—the advantage of genes-in-pieces
- 3.7 Alternative splicing—a major source of domain-based protein diversity
- References
- 4. How one structure has changed a field—the major histocompatibility complex molecules in cellular immunity
- Abstract
- 4.1 What is the evolutionary driving force behind “histocompatibility”?
- 4.2 The class I and class II major histocompatibility complex molecules
- 4.3 The quest to solve the first class I major histocompatibility complex structure had a difficult start
- 4.4 Phase ambiguity and the mystery of “extra” electron density
- 4.5 A bombshell
- 4.6 The demanding class II major histocompatibility complex journey
- 4.7 Distinct peptide-binding modes of two major histocompatibility complex molecules
- 4.8 The polymorphic binding pockets
- 4.9 The killer versus the helper
- 4.10 Major histocompatibility complex structures in species perpetuation
- References
- 5. T cell receptors, the molecular bodyguard in αβ T lymphocyte immunity
- Abstract
- 5.1 Early days of cellular immunology—the search for a T cell receptor
- 5.2 The first wave of T cell receptor structural biology
- 5.3 The Wang/Reinherz endeavor—an example of the difficulty of TCR structural biology
- 5.4 The similarities and differences of two antigen-specific receptors: T cell receptor versus antibody
- 5.5 The biology of T cell receptor-pMHC docking
- 5.6 CD3, CD4, and CD8—not just accessory molecules for the T cell receptor
- 5.7 A full αβTCR complex is resolved
- 5.8 Puzzle one: How can the extremely weak TCR-pMHC engagement trigger an exquisitely specific and sensitive immune response?
- 5.9 Puzzle two: How can naïve T cells, trained in the thymus by self-pMHC, recognize foreign antigens that are never encountered before?
- References
- 6. Protein-mediated cell–cell interactions in multicellular biology
- Abstract
- 6.1 Four major classes of cell adhesion receptors
- 6.2 The physical character of cell adhesion manifested in the structure of hetero-adhesion pair CD2–CD58 and its immunological significance
- 6.3 The sophistication of bidirectional signaling receptors, the integrin family
- 6.4 Integrin activation: Will the integrin please stand up?
- 6.5 Integrin activation: A concerted action of outside-in and inside-out signaling?
- 6.6 The physiology of cell adhesion—from leukocyte recruitment to fertilization
- References
- 7. How do viruses assemble and infect their host cells?
- Abstract
- 7.1 Structures of spherical viruses
- 7.2 Hemagglutinin, the key player of the influenza virus in the initiation of infection
- 7.3 gp160, the HIV spike glycoprotein and its receptor interaction
- 7.4 Some structural aspects of how viruses have evolved to use cell surface molecules as viral receptors, causing human diseases
- References
- 8. AlphaFold, the successful prediction of three-dimensional protein structures and its impact on structural biology
- Abstract
- 8.1 The protein folding problem and Levinthal paradox
- 8.2 Early efforts in protein structure prediction
- 8.3 Coevolving pairs provide residue-residue proximity constraints—the genetic basis of three-dimensional structure prediction
- 8.4 Deep learning—the computational basis of AlphaFold
- 8.5 The AlphaFold2 architecture
- 8.6 AlphaFold2 applications
- 8.7 AlphaFold3, a substantially upgraded version of AlphaFold for protein interactions
- References
- Photos
- Index
- Edition: 1
- Published: November 25, 2024
- No. of pages (Paperback): 378
- No. of pages (eBook): 210
- Imprint: Academic Press
- Language: English
- Paperback ISBN: 9780323998932
- eBook ISBN: 9780323999502
JW
Jia-huai Wang
Jia-huai Wang is Associate professor at the Dana-Farber Cancer Institute, Harvard Medical School, USA. As a veteran structural biologist specialized in cell surface receptors functioning in immune system and nervous system he has around 140 peer-reviewed papers published, including 11 articles in Nature, Science and Cell. When in China, in the early 1970’s, he was the team member which determined the structure of insulin, one of the world’s first dozen protein structures solved. Since 1988 he has been working at Harvard. As a leading author, he has published a series of extremely important structures, such as the first virus receptor structure CD4, the first cell adhesion interacting complex CD2/CD58, the ground-breaking preTCR-ligand interacting complex and the prototypical axon guidance cue netrin-1 interactions. He has a deep understanding about protein structure and how a protein functions.
Affiliations and expertise
Department of Medical Oncology and Department of Cancer Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, USARead Proteins on ScienceDirect