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Atomic Force Microscopic Electron Spectroscopic Imaging And Molecular Simulation Investigations Of The Assembly And Structures Of Collagen Constructs
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Book Synopsis Atomic Force Microscopic, Electron Spectroscopic Imaging and Molecular Simulation Investigations of the Assembly and Structures of Collagen Constructs by : Ning Su
Download or read book Atomic Force Microscopic, Electron Spectroscopic Imaging and Molecular Simulation Investigations of the Assembly and Structures of Collagen Constructs written by Ning Su and published by . This book was released on 2013 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis AFM, ESI and Molecular Simulation Investigations of the Assembly and Structures of Collagen Constructs by : Ning Su
Download or read book AFM, ESI and Molecular Simulation Investigations of the Assembly and Structures of Collagen Constructs written by Ning Su and published by . This book was released on 2013 with total page 344 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Bridging the Hierarchical Structures of Collagen by Atomic Force Microscopy: From Nanoscale to Mesoscale by : Ming Sun
Download or read book Bridging the Hierarchical Structures of Collagen by Atomic Force Microscopy: From Nanoscale to Mesoscale written by Ming Sun and published by . This book was released on 2006 with total page 170 pages. Available in PDF, EPUB and Kindle. Book excerpt: The most abundant structural protein in mammalian tissues, Type I Collagen monomer, a long rope of 300 nm in length and 1.5 nm in diameter, can self assemble into different three-dimensional structures with multiple functions as diverse as transparent cornea, tough tendon, and strong bone. Although the microscopic structure of the monomer and the macroscopic structures of some higher hierarchical assembled fibrils have been characterized during the past years, the formation of these higher hierarchical structures, and the emergence of their bioactivities on the nano-to-mesoscale, are still not so clear. In our work, AFM (atomic force microscopy) was applied in vitro, primarily as a imaging tool to investigate the self assembled protofibril patterns (bottom-up method), and also as a 'molecular broom' to create monomer bundle patterns under appropriate force (top-down method). We believe those unique discoveries in our lab will definitely cast light on the understanding of the in vivo self-assembly and related structure-property relationships of collagen, and provide a functional surface coating method for tissue engineering and cell study.
Book Synopsis Mechanical Studies of Single Collagen Molecules Using Imaging and Force Spectroscopy by : Naghmeh Rezaei
Download or read book Mechanical Studies of Single Collagen Molecules Using Imaging and Force Spectroscopy written by Naghmeh Rezaei and published by . This book was released on 2016 with total page 97 pages. Available in PDF, EPUB and Kindle. Book excerpt: Collagen is a key component of the extracellular matrix and is the most abundant protein in vertebrates. Collagen is found in almost every connective tissue of the body including skin, bone, tendon, cartilage, arteries and cornea, where it plays a crucial role in providing structural support. Collagen molecules self-assemble to form hierarchical structures, from single molecules to fibrils to fibers and tissues. Structural and mechanical changes at the molecular level may affect self-assembly of the molecules and the resulting tissue. Despite its significance, the mechanics of collagen and its flexibility at the molecular level remain contentious, and collagen has been variously described as a flexible polymer to a semi-rigid rod. In this thesis, I present my work developing and utilizing experimental and analytical tools to study the mechanical proprieties of molecular collagen. I carefully designed and controlled a wide variety of experimental conditions, such as different collagen types and sources, solution pH and salt concentrations, and analysed the results in search of potential reasons for inconsistency in reported results of collagen flexibility at the basic molecular level. Atomic force microscopy (AFM) imaging is used to study effect of environmental factors such as ionic strength and pH on molecular conformations and flexibility of single collagen molecules. In addition, molecular conformations of different types of collagen from different sources are compared using AFM imaging. I measure persistence length of collagen molecules, a measure of flexibility, arising due to the conformational sampling of collagen. My results link the bending energy of collagen molecules to how tightly the helix is wound. In order to analyse AFM images of collagen, I developed an image and statistical analysis algorithm, SmarTrace, optimized for my images of collagen. The program was validated using images of DNA with known persistence length, then applied to collagen molecules. Analysis of different types of collagen in two different solutions and type I collagen in solutions of different ionic strength and pH show that collagen's flexibility depends strongly on ionic strength and pH. In addition, it shows that different types of collagen show similar average conformational characteristics in a given solution environment. In addition, mechanical properties and force-response of single collagen and procollagen molecules are studied using optical tweezers. I discuss the challenges of stretching single collagen proteins, whose length is much less than the size of the microspheres used as manipulation handles, and show how instrumental design and biochemistry can be used to overcome these challenges. The result of this work is an improved understanding of the sensitivity of molecular flexibility, stability and response of collagen to environmental factors. This can shed light on identifying underlying mechanisms of collagen-related diseases as well as designing and producing improved engineered biomaterials with tunable properties.
Book Synopsis Electron Microscope Investigations of the Structure of Collagen by :
Download or read book Electron Microscope Investigations of the Structure of Collagen written by and published by Ardent Media. This book was released on with total page 24 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Ultrastructure of the Connective Tissue Matrix by : P. Motta
Download or read book Ultrastructure of the Connective Tissue Matrix written by P. Motta and published by Springer Science & Business Media. This book was released on 2012-12-06 with total page 224 pages. Available in PDF, EPUB and Kindle. Book excerpt: In recent years, the techniques of electron microscopy have developed so widely and rapidly that they now cover the fields of research once the unique ll:panage of sister research techniques such as biochemistry, physiology, immunology, X-ray diffraction, etc. It is now possible to reach molecular and submolecular levels, making this technique indispensable in every type of research. Electron microscopy alone often provides enough information to solve given problems. In the field of the connective tissue matrix, knowledge of the molecular structure of collagen, pro teoglycans and elastin and their interaction has been to a large extent elucidated by electron microscopy. The field over which electron microscopy ranges in the investigation of the connective tissue matrix is so wide that the aim of this volume is to collect the main ultrastructural acquisitions disseminated in various journals and monographs in one book. The intent ofthis volume is to: (a) integrate different and new microscopic methods and review the results of such an integrative approach; (b) present a comprehensive ultrastructural account of selected aspects of the field; (c) point out gaps or controversial topics in our knowledge; (d) outline pertinent future research and expansion of the subject.
Download or read book Collagen written by Marcel E. Nimni and published by CRC Press. This book was released on 2018-01-18 with total page 516 pages. Available in PDF, EPUB and Kindle. Book excerpt: This series was conceived with the idea of integrating current aspects of ongoing research in the collagen field. The book consists of a spectrum of papers which discus divers aspects such as X-ray structure, the thermodynamics and mechanism of fibrillogenesis, and the use of collagen as a biomaterial for the manufacturing of many implantable, sometimes lifesaving, devises.
Book Synopsis Atomic Force Microscopy Studies of Fibrous Long Spacing Type Collagen Aggregates Formed In-vitro: Self-assembly, Structure and Stability by : Chuck Kaung Wen
Download or read book Atomic Force Microscopy Studies of Fibrous Long Spacing Type Collagen Aggregates Formed In-vitro: Self-assembly, Structure and Stability written by Chuck Kaung Wen and published by . This book was released on 2003 with total page 488 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Author :Jan Kristian Rainey Publisher :National Library of Canada = Bibliothèque nationale du Canada ISBN 13 :9780612783102 Total Pages :518 pages Book Rating :4.7/5 (831 download)
Book Synopsis Collagen Structure and Preferential Assembly Explored by Parallel Microscopy and Bioinformatics [microform] by : Jan Kristian Rainey
Download or read book Collagen Structure and Preferential Assembly Explored by Parallel Microscopy and Bioinformatics [microform] written by Jan Kristian Rainey and published by National Library of Canada = Bibliothèque nationale du Canada. This book was released on 2003 with total page 518 pages. Available in PDF, EPUB and Kindle. Book excerpt: Although its self-assembly is ubiquitous for most animals and has been extensively studied for decades, collagen remains a rather enigmatic protein. The preferential assembly process of one particular collagen construct, fibrous long spacing collagen formed with added alpha1-acid glycoprotein, is detailed. Stable intermediate structures are resolved by atomic force microscopy, demonstrating for the first time the onset of the periodic surface protrusions separated by 270 nm that are characteristic of this form of collagen. A preliminary fibrillogenesis mechanism is proposed on the basis of this data, but the ongoing problem of the lack of a high-resolution structure for the collagen monomer makes detailed analysis difficult. Therefore, a diversion into bioinformatics styled analyses is presented. In the first analysis, the collagen triple-helix is parameterized using all available high-resolution crystal structure data. This provides a general framework for prediction of any triple-helical peptide structure and is shown using a nonredundant data set to generate a prediction agreeing exceptionally well with the highest resolution structure solved to date. From a preferential assembly standpoint, only the terminal atoms of each residue are important--it is these that modulate supramolecular assembly through either attractive or repulsive interactions. However, the large size (∼3150 amino acids) of the collagen monomer makes prediction of all side chain atoms undesirable. Following the success of backbone dependent rotamer libraries, a second statistically derived parameter set is developed. It allows prediction of terminal side-chain atom positions given only a polypeptide backbone. This is validated by comparing numerous predictions to experimental structures for a large set of protein structures, showing excellent potential as a general predictive method for efficiently positioning side-chains. Combining the two parameter sets, any triple-helical structure may be readily predicted. A model of the human type I collagen monomer is introduced and its utility is demonstrated through correlation with atomic force microscopy data. This allows both the interpretation of height data, and the clarification of the preliminary assembly mechanism proposed towards the beginning of the Thesis for fibrous long spacing collagen.
Download or read book Collagen written by Peter Fratzl and published by Springer Science & Business Media. This book was released on 2008-05-10 with total page 516 pages. Available in PDF, EPUB and Kindle. Book excerpt: Not only does this book provide a comprehensive review of current research advances in collagen structure and mechanics, it also explores this biological macromolecule’s many applications in biomaterials and tissue engineering. Readers gain an understanding of the structure and mechanical behavior of type I collagen and collagen-based tissues in vertebrates across all length scales, from the molecular (nano) to the organ (macro) level.
Book Synopsis Collagen Self-assembly by : Darren Anderson
Download or read book Collagen Self-assembly written by Darren Anderson and published by . This book was released on 2006 with total page 698 pages. Available in PDF, EPUB and Kindle. Book excerpt: Collagen is the major structural protein in mammals, and forms the basis of a variety of tissues essential for animal life, including bone, skin, teeth, cornea, tendon, and others. It self-assembles---both in vivo and in vitro---into a variety of biologically important structures, and this self-assembly process is highly dependent on solution pH, ionic strength, and the concentration of the collagen monomer. Kinetic studies demonstrating these dependencies are presented for the formation of the most important aggregate, native type collagen. The cold dissociation of collagen that does not contain complete non-helical telopeptide regions is also demonstrated. Based on these studies, five different types of collagen intermediates are identified and a partially hierarchical fibrillogenesis mechanism is proposed, along with a detailed kinetic model. In order to further understand collagen fibrillogenesis at a molecular level, a previously predicted structure of the collagen monomer is completely relaxed using condensed phase molecular dynamics simulations. For validation purposes, several experimentally solved model collagen structures are simulated in the same way, and the simulation results agree with the crystal structures to within the experimental error. Therefore, a structure of the collagen monomer is proposed that comprises the most complete model currently developed. This model forms the basis for two sets of simulations aimed at explaining the formation of several of the polymorphisms of collagen. First, a three-dimensional analysis of the interactions between collagen monomers in fibrillar aggregates is presented, including hydrophobic-hydrophobic and electrostatic interactions. An examination of these interactions as a function of overlap between monomers demonstrates the origin of the topological regularity in native type collagen. Second, a detailed molecular model for formation of segmental long spacing crystallites of collagen is presented, involving bridging of in-register collagen monomers by nucleotide triphosphate moieties at colocalized acidic and basic residues. The proposed model is confirmed using molecular mechanics and dynamics simulations.
Download or read book Collagen written by Jürgen Brinckmann and published by Springer Science & Business Media. This book was released on 2005-05-03 with total page 272 pages. Available in PDF, EPUB and Kindle. Book excerpt: J. Brinckmann: Collagens at a Glance.- J. Engel, H.P. Bächinger: Structure, Stability and Folding of the Collagen Triple Helix.- S. Ricard-Blum, F. Ruggiero, M. van der Rest: The Collagen Superfamily.- T. Koide, K. Nagata: Collagen Biosynthesis.- J. Myllyharju: Intracellular Post-Translational Modifications of Collagens.- D.S. Greenspan: Biosynthetic Processing of Collagen Molecules.- D.E. Birk, P. Bruckner: Collagen Suprastructures.- D.R. Eyre, J.-J. Wu: Collagen Cross-Links
Book Synopsis Assembly Mechanisms of Type I Collagen Aggregates by : Matthew Freeman Paige
Download or read book Assembly Mechanisms of Type I Collagen Aggregates written by Matthew Freeman Paige and published by . This book was released on 2000 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: The solution-phase association of biological molecules to form aggregates has been studied from a variety of perspectives, such as the flocculation of polymers, association of colloids and the aggregation of proteins. The latter subject has been the target of particular attention, mainly because of its importance in biomedical applications as well as its implication in diseases such as spongiform encephalopathies and Alzheimer's disease. Investigating protein aggregation at a fundamental level, however, is often complicated by the poorly defined structures of the aggregation products formed, as well as by the difficulty in working with biological systems. In this thesis, studies of Type-I collagen, a rod-like protein which can undergo 'in vitro' aggregation into highly-ordered protein structures, have been carried out with a view towards determining the mechanisms by which protein aggregates form. Two particular aggregate structures have been investigated. The first, a block-like aggregate called segmental long spacing collagen, was formed by the addition of nucleotide triphosphates to collagen monomers. By analyzing aggregate structures, formation kinetics and growth thermodynamics, it was concluded that these aggregates form via a hierarchical growth mechanism involving the formation of a stable intermediate and subsequent fusion of these intermediates. The second form of aggregate investigated was a fibril referred to as fibrous long spacing collagen. In this case, particular insight was made into elucidating the structure of these fibrils using the atomic force microscope. Results obtained again suggest that this aggregate forms via a hierarchical mechanism, first forming stable 'protofibrils', which then merge in a complex manner to produce the final structure. In the final Part of this thesis, the capabilities of the atomic force microscope in performing imaging of dynamic, biological processes in real time was examined, and was used to image the enzymatic digestion of collagen fibrils by the protein collagenase. The utility of the atomic force microscopy for 'in situ' investigation of complex processes such as collagen formation is discussed with a view towards applying this technique to future work.
Book Synopsis Structural Investigation of Type-I Collagen Fibril Using Atomic Force Microscopy by : Ning Su
Download or read book Structural Investigation of Type-I Collagen Fibril Using Atomic Force Microscopy written by Ning Su and published by . This book was released on 2008 with total page 108 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Visualizing Chemistry by : National Research Council
Download or read book Visualizing Chemistry written by National Research Council and published by National Academies Press. This book was released on 2006-06-01 with total page 222 pages. Available in PDF, EPUB and Kindle. Book excerpt: Scientists and engineers have long relied on the power of imaging techniques to help see objects invisible to the naked eye, and thus, to advance scientific knowledge. These experts are constantly pushing the limits of technology in pursuit of chemical imagingâ€"the ability to visualize molecular structures and chemical composition in time and space as actual events unfoldâ€"from the smallest dimension of a biological system to the widest expanse of a distant galaxy. Chemical imaging has a variety of applications for almost every facet of our daily lives, ranging from medical diagnosis and treatment to the study and design of material properties in new products. In addition to highlighting advances in chemical imaging that could have the greatest impact on critical problems in science and technology, Visualizing Chemistry reviews the current state of chemical imaging technology, identifies promising future developments and their applications, and suggests a research and educational agenda to enable breakthrough improvements.
Book Synopsis Molecular Scale Materials Assembly Investigated by Atomic Force Microscopy by : Kang Rae Cho
Download or read book Molecular Scale Materials Assembly Investigated by Atomic Force Microscopy written by Kang Rae Cho and published by . This book was released on 2010 with total page 316 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Collagen Assembly as Examined by Atomic Force Microscopy by : Marla Gale
Download or read book Collagen Assembly as Examined by Atomic Force Microscopy written by Marla Gale and published by . This book was released on 1995 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: The use of atomic force microscopy (AFM) to image the assembly of Type I collagen from monomers, through the various intermediates, to mature fibrils, has been demonstrated for the first time. These stages of collagen assembly were found to proceed by a stepwise process, which commenced with axially associated oligomers (height ~ 1 nm, lengths 450-1200 nm) and proceeded by lateral and axial association through intermediate microfibrils of 2-3 nm in diameter (with periodicity ~ 67 nm). Further assembly into larger microfibrils (>10,000 nm in length) that aggregated readily was observed. The end product of assembly observed in this study was a mature fibril, which demonstrated 4D-banding with a periodicity of 67 nm.
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