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SUPPORTING INFORMATION소수성 상호작용이 HubWA 단백질의 폴딩 반응에 끼치는 영향

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(1)

Journal of the Korean Chemical Society 2019, Vol. 63, No. 6

Printed in the Republic of Korea

-1-

SUPPORTING INFORMATION

소수성 상호작용이 HubWA 단백질의 폴딩 반응에 끼치는 영향

박순호

강릉원주대학교 치과대학 치의학과 생화학 및 분자생물학 (접수 2019. 7. 2; 게재확정 2019. 9. 4)

Contribution of Hydrophobic Interactions to HubWA Folding Reaction

Soon-Ho Park

Biochemistry and Molecular Biology Group, Department of Dentistry, College of Dentistry, Research Institute of Oral Sciences, Gangneung-Wonju National University,

Gangneung 25457, Korea. E-mail: [email protected] (Received July 2, 2019; Accepted September 4, 2019)

Figure S1. DNA sequence of V5A, I13A, V17A and I36A. Mutated residue is designated as asterisk.

(2)

Journal of the Korean Chemical Society

2 박순호

Figure S2. SDS-PAGE of V5A, I13A, V17A and I36A. Gels were stained by coommassie brilliant blue. Purified mutant proteins were shown as a single band.

Figure S3. Ribbon diagram of V5A, I13A, V17A and I36A. α-Carbon of mutated residue is shown as sphere and labeled in italic letter.

α-Carbons of residues that are located within 1.8 Å of mutated residue are shown as spheres and labeled in normal letter.

수치

Figure S1. DNA sequence of V5A, I13A, V17A and I36A. Mutated residue is designated as asterisk.
Figure S3. Ribbon diagram of V5A, I13A, V17A and I36A. α-Carbon of mutated residue is shown as sphere and labeled in italic letter.

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