Search
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/04%3A_Proteins-_Structure_and_Folding/4.07%3A_The_Three-Dimensional_Structure_of_Proteins/4.7.06%3A_Intrinsically_Disordered_ProteinsFigure \PageIndex9 below shows a simplified molecular dynamics simulation of the intrinsically disordered protein human alpha-synuclein (Uniprot ID P37840). (Molecular dynamics were discussed in...Figure \PageIndex9 below shows a simplified molecular dynamics simulation of the intrinsically disordered protein human alpha-synuclein (Uniprot ID P37840). (Molecular dynamics were discussed in Chapter 3.4: Analyses of Protein Structure.) α-Synuclein (140 amino acids, MW 14,460) is expressed in the brain and presynaptic terminals in the central nervous system but also in more distal neurons and is involved in the regulation of neurotransmitter release and in the synaptic vesicles that ho…
- https://bio.libretexts.org/Workbench/Biochem_Remix_Acevedo/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.02%3A_Tertiary_and_Quaternary_StructuresProteins, especially those involved in cytoskeletal filaments, can form fibers with helical symmetry which differs from those described above since the monomers at the ends of helical fibers, although...Proteins, especially those involved in cytoskeletal filaments, can form fibers with helical symmetry which differs from those described above since the monomers at the ends of helical fibers, although they have the same tertiary structures as those in the middle of the helical fibers, do not contact the same number of monomers as monomers internal in the oligomer.
- https://bio.libretexts.org/Workbench/Biochem_Remix_Acevedo/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.04%3A_Protein_with_Alpha_Alpha-Beta_Beta_and_Little_Secondary_StructureProteins can also be classified as to the type and extent of secondary structure found in the protein. Example: the Z[beta] Domain of the RNA-editing Enzyme ADAR1 (1xmk), shown in the interactive iCn3...Proteins can also be classified as to the type and extent of secondary structure found in the protein. Example: the Z[beta] Domain of the RNA-editing Enzyme ADAR1 (1xmk), shown in the interactive iCn3D model in Figure \PageIndex1. Example: The second SH3 domain from ponsin (2O9S), shown in the interactive iCn3D model in Figure \PageIndex3. Example: Human biliverdin IX beta reductase (1hdo), shown in the interactive iCn3D model in Figure \PageIndex6.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.07%3A_Fibrillar_ProteinsThe page discusses various fibrillar proteins, focusing on their structure, function, and role in biological systems. It describes different types of fibrillar proteins, such as collagen, ??-keratin, ...The page discusses various fibrillar proteins, focusing on their structure, function, and role in biological systems. It describes different types of fibrillar proteins, such as collagen, ??-keratin, elastin, and fibrinogen, and highlights their structural characteristics, including unique amino acid compositions and hierarchical organizations.
- https://bio.libretexts.org/Workbench/Biochem_Remix_Acevedo/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.03%3A_Secondary_Structural_Motifs_and_DomainsThe beta strands (yellow) and connecting alpha helices (red), and coil (blue) of the Rossman fold are shown in the context of the rest of the monomeric version of the protein, which is shown in gray. ...The beta strands (yellow) and connecting alpha helices (red), and coil (blue) of the Rossman fold are shown in the context of the rest of the monomeric version of the protein, which is shown in gray. Each β-strand connects to the next adjacent strand in the barrel through a long right-handed loop that includes one of the helices, so that the ribbon N-to-C coloring in the top view (A) proceeds in rainbow order around the barrel.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.03%3A_Tertiary_and_Quaternary_StructuresThe page discusses the fundamentals of biochemistry with a focus on tertiary and quaternary protein structures. Learning goals include distinguishing between tertiary and quaternary protein structures...The page discusses the fundamentals of biochemistry with a focus on tertiary and quaternary protein structures. Learning goals include distinguishing between tertiary and quaternary protein structures, understanding forces stabilizing tertiary structures, identifying domains and motifs, and exploring protein folding pathways. It also covers analyzing oligomerization, allosteric regulation, structural organization, interpreting structural data, and the impact of mutations on protein structures.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.06%3A_Intrinsically_Disordered_ProteinsThis page provides a comprehensive overview of Intrinsically Disordered Proteins (IDPs), detailing their characteristics, biological roles, structural dynamics, and relevance in health and disease. ID...This page provides a comprehensive overview of Intrinsically Disordered Proteins (IDPs), detailing their characteristics, biological roles, structural dynamics, and relevance in health and disease. IDPs are unique as they lack fixed three-dimensional structures but are involved in crucial cellular functions like molecular recognition and signaling. The page covers the experimental methods for identifying IDPs, evolutionary perspectives, and implications in disease and therapeutics.
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/04%3A_Proteins-_Structure_and_Folding/4.07%3A_The_Three-Dimensional_Structure_of_Proteins/4.7.04%3A_Secondary_Structural_Motifs_and_DomainsThe beta strands (yellow) connecting alpha helices (red) and coil (blue) of the Rossman fold are shown in the context of the rest of the monomeric version of the protein, which is shown in gray. Each ...The beta strands (yellow) connecting alpha helices (red) and coil (blue) of the Rossman fold are shown in the context of the rest of the monomeric version of the protein, which is shown in gray. Each β-strand connects to the next adjacent strand in the barrel through a long right-handed loop that includes one of the helices so that the ribbon N-to-C coloring in the top view (A) proceeds in rainbow order around the barrel.
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/04%3A_Proteins-_Structure_and_Folding/4.07%3A_The_Three-Dimensional_Structure_of_Proteins/4.7.05%3A_Protein_with_Alpha_Alpha-Beta_Beta_and_Little_Secondary_StructureIn summary, this chapter illustrates that despite the complexity of protein structures, a relatively limited set of structural motifs and architectures recur across different proteins, providing insig...In summary, this chapter illustrates that despite the complexity of protein structures, a relatively limited set of structural motifs and architectures recur across different proteins, providing insight into their function, evolution, and the principles governing protein folding and assembly.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.05%3A_Protein_with_Alpha_Alpha-Beta_Beta_and_Little_Secondary_StructureThe page outlines learning goals related to understanding protein structure, emphasizing the classification of proteins based on their secondary structure. It guides students to distinguish between ma...The page outlines learning goals related to understanding protein structure, emphasizing the classification of proteins based on their secondary structure. It guides students to distinguish between major classes of protein folds, examining the role of ??-helices, ??-sheets, and disordered regions in shaping protein topology and function.
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/04%3A_Proteins-_Structure_and_Folding/4.07%3A_The_Three-Dimensional_Structure_of_Proteins/4.7.07%3A_Fibrillar_ProteinsIn arthropods, resilin is largely involved in a number of different functions, including the flexibility and deformability of membranous cuticle and joint systems, the storage of elastic energy in loc...In arthropods, resilin is largely involved in a number of different functions, including the flexibility and deformability of membranous cuticle and joint systems, the storage of elastic energy in locomotion (jumping, flying, etc.) and catapulting systems, the adaptability to surface topography by multiple contact attachment, and prey catching systems and the reduction of fatigue and damage in feeding and traumatic reproductive system.
