STUDY OF THE MECHANISM OF 12C（d,d）12C AND 12C（d,p）13C* REACTIONS

A formalism for studying the interference between the direct reaction and the compound resonance processes is presented by the S-matrix theory; The mechanism of ¹²C（d, d） ¹²C, ¹²C（d, p₁） ¹³C* and ¹²C（d, p₂） ¹³C* reactions in the energy range E_d=1.63 MeV to 2.05 MeV is analysed.Te results show that: the interference between these two processes exists; and the quantitative relation between them is given. While the parameters of direct reactions and compound resonance processes, particularly for four resonance states with E_d=1.726, 1.767, 1.792 and 1.86 MeV are determined.     

Combining rule for interaction energies of the (CO)2, (N2)2 and CO-N2 complexes

The relationship between interaction energies of the most stable structures of the (CO)₂, (N₂)₂ and CO-N₂ complexes is investigated using the supermolecule CCSD(T) and MP4 methods and aug-cc-pVXZ (X = D,T,Q) basis sets extended by a set of midbond functions centred in the middle of the intermolecular bond. A simple combining rule for interaction energies of this triad of clusters is proposed.     

ADSORPTION DYNAMICS OF MACROPOROUS POLYMERIC ADSORBENT Ⅱ. The Studies on the Film Diffusion Mass-Transfer Process

1 INTRODUCTIONAt present time, most of the studies for the adsorption dynamics of macroporous adsorbent,.especially for the film diffusion mass-transfer process, were based on the conclusions for theBoyd ion-exchange dynamics equationl'l. The structure of gel-type ion-exchange resin andmacroporous polystyrene resin is different. Because of having the hydrophilic group, both of theirmer and outer of the ion-exchange resin can swell to the reticulation struCture in the aqueous.Based on the…     

Semisynthesis and folding of the potassium channel KcsA

In this contribution we describe the semisynthesis of the potassium channel, KcsA. A truncated form of KcsA, comprising the first 125 amino acids of the 160-amino acid protein, was synthesized using expressed protein ligation. This truncated form corresponds to the entire membrane-spanning region of the protein and is similar to the construct previously used in crystallographic studies on the KcsA protein. The ligation reaction was carried out using an N-terminal recombinant peptide alpha-thioester, corresponding to residues 1-73 of KcsA, and a synthetic C-terminal peptide corresponding to residues 74-125. Chemical synthesis of the C-peptide was accomplished by optimized Boc-SPPS techniques. A dual fusion strategy, involving glutathione-S-transferase (GST) and the GyrA intein, was developed for recombinant expression of the N-peptide alpha-thioester. The fusion protein, expressed in the insoluble form as inclusion bodies, was refolded and then cleaved successively to remove the GST tag and the intein, thereby releasing the N-peptide alpha-thioester. Following chemical ligation, the KcsA polypeptide was folded into the tetrameric state by incorporation into lipid vesicles. The correctness of the folded state was verified by the ability of the KcsA tetramer to bind to agitoxin-2. To our knowledge, this work represents the first reported semisynthesis of a polytopic membrane protein and highlights the potential application of native chemical ligation and expressed protein ligation for the (semi)synthesis of integral membrane proteins.     

Structural and functional consequences of an amide-to-ester substitution in the selectivity filter of a potassium channel

The selectivity filter of K(+) channels comprises four contiguous ion binding sites, S1 through S4. Structural and functional data indicate that the filter contains on average two K(+) ions at any given time and that these ions reside primarily in two configurations, namely to sites S1 and S3 or to sites S2 and S4. Maximum ion flux through the channel is expected to occur when the energy difference between these two binding configurations is zero. In this study, we have used protein semisynthesis to selectively perturb site 1 within the filter of the KcsA channel through use of an amide-to-ester substitution. The modification alters K(+) conduction properties. The structure of the selectivity filter is largely unperturbed by the modification, despite the loss of an ordered water molecule normally located just behind the filter. Introduction of the ester moiety was found to alter the distribution of K(+), Rb(+,) and Cs(+) within the filter, with the most dramatic change found for Rb(+). The redistribution of ions is associated with the appearance of a partially hydrated ion just external to the filter, at a position where no ion is observed in the wild-type channel. The appearance of this new ion-binding site creates a change in the distance between a pair of K(+) ions some fraction of the time, apparently leading to a reduction in the ion conduction rate. Importantly, this finding suggests that the selectivity filter of a potassium channel is optimized both in terms of absolute ion occupancy and in terms of the separation in distance between the conducting ions.