UB Paderborn / Katalog / Suche / in CDI

[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves

Methods in Enzymology, 1986, Vol.131, p.266-280

Pace, C.N.

1986

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Hydrogen bonding stabilizes globular proteins

Biophysical journal, 1996-10, Vol.71 (4), p.2033-2039

1996

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Organophosphorus Hydrolase Is a Remarkably Stable Enzyme That Unfolds through a Homodimeric Intermediate

Biochemistry (Easton), 1997-11, Vol.36 (47), p.14366-14374

1997

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[24] Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding

Methods in Enzymology, 1995, Vol.259, p.538-554

Pace, C.N.

1995

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Conformational stability of ribonuclease T1 determined by hydrogen‐deuterium exchange

Protein science, 1997-07, Vol.6 (7), p.1387-1395

1997

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Energetics of ribonuclease T1 structure

Biochemistry (Easton), 1994-03, Vol.33 (11), p.3312-3319

1994

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The disulphide folding pathway of ribonuclease T 1

Journal of molecular biology, 1986, Vol.188 (3), p.477-486

1986

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Inhibition of pepsinogen activation by gossypol

The Journal of biological chemistry, 1970-12, Vol.245 (23), p.6456-6461

1970

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Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation

The Journal of biological chemistry, 1980-05, Vol.255 (9), p.3862-3865

1980

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The disulphide folding pathway of ribonuclease T1

Journal of molecular biology, 1986-04, Vol.188 (3), p.477-486

1986

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Urea and guanidine hydrochloride denaturation of ribonucleas e, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin

The Journal of biological chemistry, 1974, Vol.249 (17), p.5388-5393

1974

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Enzyme inhibition

Trends in biochemical sciences (Amsterdam. Regular ed.), 1980-01, Vol.5 (7), p.173-174

Pace, C.N.

1980

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Protein conformations and their stability [Food science]

Journal of the American Oil Chemists' Society, 1983-05, Vol.60 (5), p.970-975

Pace, C. N.

1983

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A comparison of the effectiveness of protein denaturants for β-lactoglobulin and ribonuclease

Archives of biochemistry and biophysics, 1980, Vol.199 (1), p.270-276

1980

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Purification and partial characterization of alcohol dehydrogenase from wheat

Archives of biochemistry and biophysics, 1979-09, Vol.196 (2), p.611-618

1979

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Wheat alcohol dehydrogenase isozymes: purification, characterization, and gene expression

Plant physiology (Bethesda), 1980-03, Vol.65 (3), p.518-522

1980

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[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves

Hydrogen bonding stabilizes globular proteins

Organophosphorus Hydrolase Is a Remarkably Stable Enzyme That Unfolds through a Homodimeric Intermediate

[24] Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding

Conformational stability of ribonuclease T1 determined by hydrogen‐deuterium exchange

Energetics of ribonuclease T1 structure

The disulphide folding pathway of ribonuclease T 1

Inhibition of pepsinogen activation by gossypol

Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation

The disulphide folding pathway of ribonuclease T1

Urea and guanidine hydrochloride denaturation of ribonucleas e, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin

Enzyme inhibition

Protein conformations and their stability [Food science]

A comparison of the effectiveness of protein denaturants for β-lactoglobulin and ribonuclease

Purification and partial characterization of alcohol dehydrogenase from wheat

Wheat alcohol dehydrogenase isozymes: purification, characterization, and gene expression

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