• 한국결정성장학회지
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• 제21권4호
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• pp.153-157
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• 2011

Inductively Coupled Plasma(ICP)를 이용하여 다양한 조건으로 표면 처리한 Si(100) 기관 위에 Low Pressure Chemical Vapor Deposition(LPCVD)를 이용하여 Ge 층을 이종접합 성장하고, Ge 층 성장 초기의 표면 상태를 Scanning Electron Microscopy(SEM)을 통해 분석하였다. ICP를 이용하여 표면 처리된 Si(100) 기판 위에 성장된 Ge 층의 경우 ICP 처리하지 않은 시편보다 Ge 성장율이 약 5배 이상 증가되었다. ICP 처리된 시편의 Ge 성장률 증가는 ICP 표면 처리 공정으로 Si 기관 표면에서 떨어져 나간 missing dimer가 Ge adatom들에 핵을 형성할 자리를 제공하여 Ge island의 형성과 융합을 촉진시키는 것으로 사료된다.

• 한국진공학회:학술대회논문집
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• 한국진공학회 2009년도 제38회 동계학술대회 초록집
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• pp.364-364
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• 2010

Defects existing on the clean Si(5 5 12)-$2{\times}1$, composed of one-dimensional(1-D) structures such as honeycomb (H) chain, $\pi$-bonded ($\pi$) chains, dimer-adatom (D-A) row, and tetramer (T) row, have been investigated by scanning tunneling microscopy (STM). It is found that the defects can be classified to two categories: One is originated from phase boundaries in D-A and T rows having $2{\times}$ periodicities, by which buckling directions are reversed, and the other is caused by missing atoms on $\pi$ chains, D-A rows, and T rows. All these defects are symmetric with respect to the [6 6 $\bar{5}$] direction, which is due to one-dimensional symmetry along the [1 $\bar{1}$ 0] direction. Especially it is worth noticing that on H chains none of such defects exist, which implies that the H chain is energetically the most stable among 1-D structures existing on Si(5 5 12)-$2{\times}1$.

• BMB Reports
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• 제38권1호
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• pp.58-64
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• 2005

Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the IMPP from a porcine brain with pyridoxal-5'-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff's base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-1-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.