It follows that the possibility of structural classification of globular proteins (domains) does not imply the existence of a correlation in protein primary structure. This possibility exists even in random sequences of amino acid residues and therefore may not be the result of biological evolution....
protein- Pronounced PRO-teen or PRO-tee-un, it comes from Greek proteios, "primary," as these compounds are essential to all living organisms. protoplasm- A mixture of organic and inorganic substances, such as protein and water, it is regarded as the physical basis of life. ...
Determining function of a protein from its primary structure is among the most important problems in molecular biology. The usual approach – inferring function from homology – requires detailed description of functional units, considerable amount of data and is computationally rather demanding. Instead,...
For this we studied the polyQ tract of the TATA-box binding protein (TBP), which has a primary structure that suggests the presence of an electrostatic interaction between either of two Glu residues immediately flanking the tract at the N-terminus (Glu9 and Glu10) and an Arg interrupting it...
Structure & function of myoglobin1. Present in heart & skeletal muscle.2. As an oxygen reservoir & carrier.3. 17.8kDa,153AAs single chain, the globular heme-protein.-B-1.-Helical 9、 content of myoglobin -B-2. Location of polar & nonpolar AAs -B-3. Binding of the hemeIn the ...
Protein structures are dynamic, undergoing motions that can play a vital role in function. However, the link between primary sequence and conformational dynamics remains poorly understood. Here, we studied how conformational dynamics can arise in a globular protein by evaluating the impact of ...
between partners that are close in sequence, the primary exception being hydrogen-bonded ion pairs. (2) Most hydrogen bonds are between backbone atoms in the protein, an average of 68%. (3) All proteins studied have extensive hydrogen-bonded secondary structure, an average of 82%. (4) ...
C1q is a versatile recognition protein that binds to an amazing variety of immune and non-immune ligands and triggers activation of the classical pathway of complement. The crystal structure of the C1q globular domain responsible for its recognition properties has now been solved and refined to ...
Thus, these systems may aid in the elucidation of the rules governing protein folding from a given primary sequence; in particular, the interplay of short- vs long-range interaction can be explored. Three distinct models (AC) were examined. In model A, in addition to the preference for ...
We find that although most residues within APRs are in a structural gridlock coupling aggregation and thermodynamic stability, specific positions in a protein structure can be mutated to lower the aggregation propensity of the primary sequence without significantly affecting protein stability. These context...