• Proceedings of the Korea Information Processing Society Conference
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• 2007.05a
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• pp.10-13
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• 2007

모티프는 진화과정을 거치면서 단백질 서열상에서 부분적으로 높게 보존된 지역을 의미한다. 이러한 모티프는 단백질의 기능과 구조를 예측하거나 생물학적으로 관련성이 있는 단백질의 공통적인 특성을 기술하는데 사용된다. 또한, 모티프와 단백질 서열의 상관관계는 생물학적 기능 예측에 필수적이며, 이러한 예측 문제는 모티프 검색을 통해 서열에 존재하는 빈발한 서열패턴과 구조패턴을 통해 단백질 서열에 대한 분석이 가능하다. 이 논문에서는 단백질 서열에 존재하는 2차 구조 특성과 빈발패턴을 검색하고 추출된 정보를 이용하여 단백질 기능 분류에 활용하고자 한다.

• Korean Journal of Food Science and Technology
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• v.25 no.5
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• pp.521-525
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• 1993

To elucidate adsorption of proteins and examine the molecular behavior of protein molecules at interfaces, various proteins at the air-water interface were studied. The adsorption data of bovine serum albumin intermediates indicated that the conformational state of a protein played an important role in adsorption of proteins at interfaces. The adsorption behavior of succinylated beta-lactoglobulin indicated that the increase in the net negative charge of the protein significantly inflenced both the kinetics and thermodynamics of adsorption. The adsorption kinetics of beta-casein showed that the salt that induced break-down of water structure decreased the rate of adsorption.

• Journal of Life Science
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• v.10 no.3
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• pp.279-285
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• 2000

CRP (cyclic AMP receptor protein) regulate transcription of catabolite-sensitive genes in Escherichia coli. Wild-type and mutant CRP (S83G and S128A) proteins were used to measure the thermal stability and the temperature-dependent structural change by proteolytic digestion, UV spectrophotometer and CD spectrapolarimeter. The result indicated that wild-type CRP was more thermally stable than the mutant CRPs in the presence of cAMP. At a low temperature, wild-type CRP with cAMP was more sensitive to subtilisin than the mutant CRPs. At a high temperature, there was no difference of sensitivity to subtilisin among wild-type, S83G and S128A CRPs. CD spectra suggested that the secondary structure of CRP was destroyed partially at a high temperature.

• Korean Journal of Microbiology
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• v.53 no.4
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• pp.297-303
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• 2017

Leucine-responsive regulatory protein (LRP) is a regulatory protein of molecular weight 18.8 kDa and is widely known to regulate many metabolic and functional activities of operons in Escherichia coli. The gene for Lrp from Escherichia coli in pQE system of 6 ${\times}$ His-tagging was expressed and $^3H$-labeled protein, as well as the wild type Lrp, was purified. The crosslink experiments were performed to analyze the quaternary structure of Lrp at high of $5{\mu}M$ and at low concentrations below $0.3{\mu}M$ with cross linkers, such as glutaraldehyde, 1, 2, 3, 4-diepoxy-butane (DEB), and ethylene glycol bis (succinimidyl succinate) (EGS). In the experiments, we found that the Lrp protein can be formed higher conformation states of tetramer, hexamer, octamer, as well as dimeric state when incubated with the above cross linkers.

• The KIPS Transactions:PartD
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• v.19D no.1
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• pp.21-28
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• 2012

Predication of protein interaction sites for monomer structures can reduce the search space for protein docking and has been regarded as very significant for predicting unknown functions of proteins from their interacting proteins whose functions are known. In the other hand, the prediction of interaction sites has been limited in crystallizing weakly interacting complexes which are transient and do not form the complexes stable enough for obtaining experimental structures by crystallization or even NMR for the most important protein-protein interactions. This work reports the calculation of 3D surface patches of complex structures and their properties and a machine learning approach to build a predictive model for the 3D surface patches in interaction and non-interaction sites using support vector machine. To overcome classification problems for class imbalanced data, we employed an under-sampling technique. 9 properties of the patches were calculated from amino acid compositions and secondary structure elements. With 10 fold cross validation, the predictive model built from SVM achieved an accuracy of 92.7% for classification of 3D patches in interaction and non-interaction sites from 147 complexes.

• Proceedings of the Korean Fiber Society Conference
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• 2003.04a
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• pp.293-294
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• 2003

견 피브로인은 대표적인 섬유상 단백질의 하나로 생체적합성, 생분해성, 저독성 등의 유용한 특성을 가지므로 생체재료로 상당한 관심과 연구의 대상이 되어왔다. 우리는 최근의 연구에서 견 피브로인을 생사로부터 추출한 다음, 포름산을 용제로 하여 전기방사함으로써 나노섬유를 제조하고 이들의 각화세포에 대한 친화력을 확인한 바 있다. 본 연구에서는 견 피브로인의 구조체를 나노섬유 부직포, 필름, 마이크로 섬유로 구성된 직물 둥의 형태로 하여 그들의 2차 구조를 비교함과 동시에 구조적 특성이 각화세포와의 친화력에 어떠한 영향을 미치는 가를 비교ㆍ검토 하고자 하였다. (중략)

• Journal of the Korean Chemical Society
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• v.67 no.2
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• pp.81-88
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• 2023

The contribution of hydrophobic residues to the protein folding reaction was studied by using HubWA variant proteins with I and L to V mutation. Folding kinetics of all V variant proteins was observed to be satisfied by a three-state on-pathway mechanism, U ⇌ I ⇌ N, where U, I, and N represent unfolded, intermediate, and native state, respectively. Three-state folding reaction was quantitatively analyzed and the free energy of folding of each elementary reactions and overall folding reaction, ΔG^o_UI, ΔG^o_IN, and ΔG^o_UN, were obtained. From the ratio of free energy difference between the variant protein and HubWA, ΔΔG^o_UI/ΔΔG^o_UN (ΔΔG^o_UI = ΔG^o_UI (variant protein) - ΔG^o_UI (HubWA) and ΔΔG^o_UN = ΔG^o_UN (variant protein) - ΔG^o_UN(HubWA)), the contribution of hydrophobic residues to HubWA folding was analyzed. The residues which are located in the hydrophobic core between α-helix and β-sheet, I3, I13, L15, I30, L43, I61 and L67, showed ΔΔG^o_UI/ΔΔG^o_UN value of ~0.5 when each of these residues was mutated to V, indicating that these residues form relatively solid hydrophobic core in the intermediate state. Residues located at the end of secondary structures and loop, I23, L69 and I36 showed ΔΔG^o_UI/ΔΔG^o_UN value below 0.4 when each of these residues was mutated to V, indicating that the region containing these residues are loosely formed in the intermediate state. V17A, L50V and L56V showed fairly high ΔΔG^o_UI/ΔΔG^o_UN value of ~0.8. Since L50 and L56 are located in the region containing long loop (residue 46 to 62), it is suggested that the high ΔΔG^o_UI/ΔΔG^o_UN value of these residues prevents the formation of aggregate at the early stage of folding reaction.

• Journal of Life Science
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• v.8 no.2
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• pp.223-233
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• 1998

Discovery of molecular chaperone has stimulate cell biologists and thus made it possible to re-examine the processes whereby proteins achieve and maintain their functional conformations within living cells. the term ‘Molecular chaperone’ was first coined to describe one particular protein involved in the assembly of nucleosomes, but the term has now been extended to describe the function of a wide variety of proteins that assist protein transport across membranes, folding of nascent polypeptide, the assembly and disassembly of oligomeric structures, and the recovery or removal of proteins damaged by various environmental stresses including heat shock. Progress of molecular chaperone research is still limited by the lack of 3-dimensional structural information and detailed interacts with taget proteins in the cell. However, several laboratories around the world are attempting to extend our knowledge on the functions of molecular chaperone, and such efforts seem justified to finally provide the answers to the most burning questions shortly.

• Korean Chemical Engineering Research
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• v.46 no.3
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• pp.529-534
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• 2008

The normal shell and the regenerated oyster shell, Crassostrea gigas, are separated according to the characteristics of inner shell morphology. To study characteristics of chitin obtained from the regenerated shell, chitin prepared by acid and alkali process is analyzed by FT-IR (Fourier transform infrared spectrometer) and XRD (X-ray Diffractometer). The content of insoluble protein in the normal shell was more than doubled as compared with that in the regenerated shell. A comparison of secondary structure of the normal shell and the regenerated shell revealed that the content of random of the regenerated shell was above 47%, indicating an amount in the structural unordered state. Through amino acid composition analysis and secondary protein structure of soluble protein isolated from the normal shell and the regenerated shell, it was found that there are differences in biomineralization strategy of the regenerated shell as compared to the normal shell. The relatively low hardness of the regenerated shell is caused by the change of amino acid composition and ordered secondary protein structure as compared to hardness of the normal shell.

• The Korean Journal of Zoology
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• v.38 no.3
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• pp.417-425
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• 1995

The present study was carried out to investigate the effect of microwave fixation in comparison with that of chemical fixation in preparing the microscopic samples. The microwave fixator was equipped with infrared-temperature sensor, and that was designed to compensate air temperature in the microwave fixator. In the microwave fixation, rat tongue was well preserved in terms of muscular fasciculus and pancreas stained by Feulgen reagents showed clear reaction products in the nucleus. Reaction products by PAS method in duodenal villi appeared specifically at the goblet cells. In electron microscopy, pancreatic cellular components such as secretory granules and collagen bundles were well preserved in both fixations. In aspect of histochemical reaction and electron microscopy, high quality was due to the protein content of microwave fixed specimen. The microwave fixation method saved total duration engaging microscopic preparation.