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Schematic diagram of the 2D structure of aquaporin 1 depicting the six transmembrane alpha-helices and the five interhelical loop regions A-E The 3D structure of aquaporin Z highlighting the 'hourglass'-shaped water channel that cuts through the center of the protein. Aquaporin proteins are composed of a bundle of six transmembrane α-helices ...
[3] [4] The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a protein can be determined by methods such as Edman degradation or tandem mass spectrometry. Often, however, it is read directly from the sequence of the gene using the genetic code.
Aquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene.. AQP-1 is a widely expressed water channel, whose physiological function has been most thoroughly characterized in the kidney.
The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. [1] [2] A number of these structures may bind to each other, forming a quaternary ...
Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry. [citation needed] The activities and structures of proteins may be examined in vitro, in vivo, and in silico.
Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. [1] There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. [2]
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Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.