STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR

SCHWARZ H, HINZ HJ, MEHLICH A, Tschesche H, Wenzel H (1987)
BIOCHEMISTRY 26(12): 3544-3551.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
SCHWARZ, H; HINZ, HJ; MEHLICH, A; Tschesche, HaraldUniBi; Wenzel, HerbertUniBi
Einrichtung
Fakultät für Chemie > Biochemie I
Erscheinungsjahr
1987
Zeitschriftentitel
BIOCHEMISTRY
Band
26
Ausgabe
12
Seite(n)
3544-3551
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1655347

Zitieren

SCHWARZ H, HINZ HJ, MEHLICH A, Tschesche H, Wenzel H. STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR. BIOCHEMISTRY. 1987;26(12):3544-3551.
SCHWARZ, H., HINZ, H. J., MEHLICH, A., Tschesche, H., & Wenzel, H. (1987). STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR. BIOCHEMISTRY, 26(12), 3544-3551. https://doi.org/10.1021/bi00386a044
SCHWARZ, H, HINZ, HJ, MEHLICH, A, Tschesche, Harald, and Wenzel, Herbert. 1987. “STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR”. BIOCHEMISTRY 26 (12): 3544-3551.
SCHWARZ, H., HINZ, H. J., MEHLICH, A., Tschesche, H., and Wenzel, H. (1987). STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR. BIOCHEMISTRY 26, 3544-3551.
SCHWARZ, H., et al., 1987. STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR. BIOCHEMISTRY, 26(12), p 3544-3551.
H. SCHWARZ, et al., “STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR”, BIOCHEMISTRY, vol. 26, 1987, pp. 3544-3551.
SCHWARZ, H., HINZ, H.J., MEHLICH, A., Tschesche, H., Wenzel, H.: STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR. BIOCHEMISTRY. 26, 3544-3551 (1987).
SCHWARZ, H, HINZ, HJ, MEHLICH, A, Tschesche, Harald, and Wenzel, Herbert. “STABILITY STUDIES ON DERIVATIVES OF THE BOVINE PANCREATIC TRYPSIN-INHIBITOR”. BIOCHEMISTRY 26.12 (1987): 3544-3551.

25 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.
Foit L, Mueller-Schickert A, Mamathambika BS, Gleiter S, Klaska CL, Ren G, Bardwell JC., Antioxid Redox Signal 14(6), 2011
PMID: 21110786
Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry.
Lin LN, Brandts JF, Brandts JM, Plotnikov V., Anal Biochem 302(1), 2002
PMID: 11846388
Toward development of a screen to identify randomly encoded, foldable sequences.
Hagihara Y, Kim PS., Proc Natl Acad Sci U S A 99(10), 2002
PMID: 11997470
Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI).
Hagihara Y, Shiraki K, Nakamura T, Uegaki K, Takagi M, Imanaka T, Yumoto N., J Biol Chem 277(52), 2002
PMID: 12393867
Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V.
Zavodszky M, Chen CW, Huang JK, Zolkiewski M, Wen L, Krishnamoorthi R., Protein Sci 10(1), 2001
PMID: 11266603
Novel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database.
Burton RE, Hunt JA, Fierke CA, Oas TG., Protein Sci 9(4), 2000
PMID: 10794421
Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments.
Welfle K, Misselwitz R, Hausdorf G, Höhne W, Welfle H., Biochim Biophys Acta 1431(1), 1999
PMID: 10209285
A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant.
Guzzi R, Sportelli L, La Rosa C, Milardi D, Grasso D, Verbeet MP, Canters GW., Biophys J 77(2), 1999
PMID: 10423449
Structure and multiple conformations of the kunitz-type domain from human type VI collagen alpha3(VI) chain in solution.
Zweckstetter M, Czisch M, Mayer U, Chu ML, Zinth W, Timpl R, Holak TA., Structure 4(2), 1996
PMID: 8805527
Mechanisms and catalysts of disulfide bond formation in proteins.
Creighton TE, Zapun A, Darby NJ., Trends Biotechnol 13(1), 1995
PMID: 7765801
The thermal unfolding of hevein, a small disulfide-rich protein.
Hernández-Arana A, Rojo-Domínguez A, Soriano-García M, Rodríguez-Romero A., Eur J Biochem 228(3), 1995
PMID: 7737158
Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis.
Yu MH, Weissman JS, Kim PS., J Mol Biol 249(2), 1995
PMID: 7540212
The liquid amide transfer model and the unfolding thermodynamics of small globular proteins.
Barone G, del Vecchio P, Giancola C, Graziano G., Int J Biol Macromol 17(5), 1995
PMID: 8580089
The contribution of cross-links to protein stability: a normal mode analysis of the configurational entropy of the native state.
Tidor B, Karplus M., Proteins 15(1), 1993
PMID: 7680808
Disulfide bonds and the stability of globular proteins.
Betz SF., Protein Sci 2(10), 1993
PMID: 8251931
Thermodynamics of BPTI folding.
Makhatadze GI, Kim KS, Woodward C, Privalov PL., Protein Sci 2(12), 1993
PMID: 7507751
Thermodynamics of unfolding of the alpha-amylase inhibitor tendamistat. Correlations between accessible surface area and heat capacity.
Renner M, Hinz HJ, Scharf M, Engels JW., J Mol Biol 223(3), 1992
PMID: 1542117
Natural protein proteinase inhibitors and their interaction with proteinases.
Bode W, Huber R., Eur J Biochem 204(2), 1992
PMID: 1541261
Characterization, stability and refolding of recombinant hirudin.
Otto A, Seckler R., Eur J Biochem 202(1), 1991
PMID: 1935981
Conformational stability of globular proteins.
Pace CN., Trends Biochem Sci 15(1), 1990
PMID: 2107612
Calorimetric study of the effect of intrachain cross-linking on lysozyme unfolding.
Segawa S, Sugihara M, Maeda T, Mitsuhisa Y, Kodama M, Seki S, Sakiyama M., Biopolymers 28(6), 1989
PMID: 2730941
Binding of basic pancreatic trypsin inhibitor and related isoinhibitors to leukocytic elastase. Determination of thermodynamic parameters.
Fioretti E, Angeletti M, Cottini MT, Ascoli F., J Mol Recognit 2(3), 1989
PMID: 2484014
Disulphide bonds and protein stability.
Creighton TE., Bioessays 8(2), 1988
PMID: 3282505
On the relevance of non-random polypeptide conformations for protein folding.
Creighton TE., Biophys Chem 31(1-2), 1988
PMID: 2466495
Folding and association of proteins.
Jaenicke R., Prog Biophys Mol Biol 49(2-3), 1987
PMID: 3327098

References

Daten bereitgestellt von Europe PubMed Central.

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 2443162
PubMed | Europe PMC

Suchen in

Google Scholar