Protein structure characteristics

Li D, Roberts R. WD-rcpcat proteins structure characteristics, biological fimetion and their involvement in human diseases. Cell Mol Life Sci 2001 58(14) 2085-2097. 

Immunogenicity of Biopharmaceuticals Dependent on Protein Structural Characteristics... 

Protein Structural characteristics Location Interactions Functions... 

The simplest motif with a specific function consists of two a helices joined by a loop region. Two such motifs, each with its own characteristic geometry and amino acid sequence requirements, have been observed as parts of many protein structures (Figure 2.12). 

Many proteins consist of two or more interacting polypeptide chains of characteristic tertiary structure, each of which is commonly referred to as a subunit of the protein. Subunit organization constitutes another level in the hierarchy of protein structure, defined as the protein s quaternary (4°) structure (Figure 5.10). Questions of quaternary structure address the various kinds of subunits within a protein molecule, the number of each, and the ways in which they interact with one another. 

Like most chemical reactions, the rates of enzyme-catalyzed reactions generally increase with increasing temperature. However, at temperatures above 50° to 60°C, enzymes typically show a decline in activity (Figure 14.12). Two effects are operating here (a) the characteristic increase in reaction rate with temperature, and (b) thermal denaturation of protein structure at higher tem-... 

The breast cancer resistance protein (BCRP) belongs to the G-branch of the ABC-transporter family (ABCG2). In contrast to most other ABC-proteins, BCRP consists of only one transmembrane domain (TDM) with one nucleotide binding fold (NBF) at its C-terminus. Because of this structural characteristic BCRP as well as other ABC-transporters with only one TMD are termed half transporters. To achieve functional activity these transporters have to form hetero- or homodimers. BCRP is involved in the multidrug resistance of certain tumors and transports endogenous compounds like cholesterol and steroid hormones. 

Chemokines are a family of small cytokines, or proteins secreted by cells. Proteins are classified as chemokines according to shared structural characteristics such as small size (8-10 kDa in size), and the presence of four... 

The general structural characteristics of ribosomes and their self-assembly process are discussed in Chapter 37. These particulate entities serve as the machinery on which the mRNA nucleotide sequence is translated into the sequence of amino acids of the specified protein. 

A primary structure represents a polypeptide as a simple linear string of amino acids. Actually, within long polypeptides, certain sections fold into sheets or twist into coils. These regions with specific structural characteristics constitute the secondary structure of the protein. Figures 13-37 and 13-38 show the two most common secondary structures. 

Solid state 13C CPMAS NMR spectra of Wheat High Molecular Weight (W.HMW) subunits show well resolved resonances identical with spectra of dry protein and peptide samples [24], Most of the amino acids side-chain resonances are found in the 0-35 ppm region followed by the alpha resonances of the most abundant amino acids glycine, glutamine and proline at chemical shifts of 42, 52 and 60 ppm, respectively, and the carbonyl carbons show a broad peak in 172-177 ppm region. The CPMAS spectra of hydrated whole HMW provides important information on the structural characteristics. 

Biophysical analysis of biomolecules like proteins, nucleic acids, or lipids utilizes intrinsic physical properties of the observed molecule itself or of an associated reporter molecule, which reflect information about structural characteristics, interactions, or reactions of the subject observed. In most cases the analysis (and the labels introduced) only interferes slightly with the interaction of interest and does not induce significant changes in the properties of the reactants. 

Protein structures are so diverse that it is sometimes difficult to assign them unambiguously to particular structural classes. Such borderline cases are, in fact, useful in that they mandate precise definition of the structural classes. In the present context, several proteins have been called //-helical although, in a strict sense, they do not fit the definitions of //-helices or //-solenoids. For example, Perutz et al. (2002) proposed a water-filled nanotube model for amyloid fibrils formed as polymers of the Asp2Glni5Lys2 peptide. This model has been called //-helical (Kishimoto et al., 2004 Merlino et al., 2006), but it differs from known //-helices in that (i) it has circular coils formed by uniform deformation of the peptide //-conformation with no turns or linear //-strands, as are usually observed in //-solenoids and (ii) it envisages a tubular structure with a water-filled axial lumen instead of the water-excluding core with tightly packed side chains that is characteristic of //-solenoids. 

Charged polysoaps (polymer micelles) combine within a molecule structural characteristics of the conventional micelles and polyelectrolytes, and supposedly adopt globular conformations in aqueous media with the hydrophobic region inside and charged groups outside as in water-soluble proteins. Thus,... 

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