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Since gSBA and rSBA both exist as tetramers with identical ligand binding specificities and macromolecular properties, the change of the mode of unfolding from a two-state process to a three-state process and the decrease of T^sub m^ by 26°C for the thermal unfolding of the protein of the kilter implicate the covalenlly linked glycans for the stability of gSBA
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For this purpose we analyzed the unfolding transitions of the medium-sized multitryptophan protein α-amylase mainly by the use of λ^sub max^-signals
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4 A), up to sixfold, whereas the onset of binding occurs at either smaller or higher ANS concentrations, indicating larger and smaller binding affinities, respectively
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2% collagenase (Sigma, type I, St
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Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1
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The four hinge regions create a flexible CaM dimer that can easily slide along or wobble over the peptide sequence allowing it to interact with the different binding sites in the interior of the CaM dimer
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The intrinsic quenching of molecular rotors makes them sensitive to intrinsic rotational relaxation, which is slowed down during binding to aggregated protein
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5 A, we present results showing that the affinity between CPM-PLCβ and Gβγ at atmospheric pressure on lipid membranes is strong and matches the K^sub d^(app) (i
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This is particularly relevant to emulsifiers, some of which have a melting point above 150[degrees]F
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Partitioning the configurational space in this way, and by providing an attractive "gutter", relying on local forces alone, to connect one diffusive subspace to the next, creates the advantageous funnel landscape when the high-dimensional structure is projected into a one- or two-dimensional space
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Each 8-ns trajectory was divided into 16, 8, and 4 blocks of non-overlapping trajectory segments of 0
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Upon binding to its ligand, TGF-[alpha] undergoes autophosphorylation and activates downstream molecules, such as ras, phosphatidylinositol 3-kinase, and mitogen-activated protein kinase
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, Marti and Kochert 1996, Wink et al
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