Search Results - "Stites, W E"
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1
Packing Is a Key Selection Factor in the Evolution of Protein Hydrophobic Cores
Published in Biochemistry (Easton) (18-12-2001)“…The energy derived from optimized van der Waals interactions in closely packed, folded proteins has been proposed to be of similar energetic magnitude to…”
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2
Higher-Order Packing Interactions in Triple and Quadruple Mutants of Staphylococcal Nuclease
Published in Biochemistry (Easton) (20-11-2001)“…Sixty-four triple and 32 quadruple mutants were constructed in the core of staphylococcal nuclease. This is the first time that a large number of multiple…”
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3
Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
Published in Biochemistry (Easton) (04-09-1990)“…To quantitate the contributions of the large hydrophobic residues in staphylococcal nuclease to the stability of its native state, single alanine and glycine…”
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4
Oxidation of buried cysteines is slow and an insignificant factor in the structural destabilization of staphylococcal nuclease caused by H2O2 exposure
Published in Amino acids (01-10-2004)“…The oxidation of buried cysteine or methionine residues can destroy the enzyme activity of a protein by disrupting structure. Engineering in such an…”
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5
Energetics of Side Chain Packing in Staphylococcal Nuclease Assessed by Exchange of Valines, Isoleucines, and Leucines
Published in Biochemistry (Easton) (20-11-2001)“…To examine the importance of side chain packing to protein stability, each of the 11 leucines in staphylococcal nuclease was substituted with isoleucine and…”
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6
The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order
Published in Journal of molecular biology (05-08-1993)“…Three mutants of staphylococcal nuclease containing a tryptophan substitution have been examined in the full length (149 residues) protein and in a large…”
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7
Evidence for strained interactions between side-chains and the polypeptide backbone
Published in Journal of molecular biology (07-01-1994)“…In most proteins, a small but significant fraction of residues adopt phi,psi angles that generate unfavorable steric interactions between side-chain atoms and…”
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8
High Apparent Dielectric Constants in the Interior of a Protein Reflect Water Penetration
Published in Biophysical journal (01-09-2000)“…A glutamic acid was buried in the hydrophobic core of staphylococcal nuclease by replacement of Val-66. Its pK a was measured with equilibrium thermodynamic…”
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9
Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability
Published in Journal of molecular biology (20-10-2000)“…Seven hyper-stable multiple mutants have been constructed in staphylococcal nuclease by various combinations of eight different stabilizing single mutants. The…”
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10
Instrumentation for Automated Determination of Protein Stability
Published in Analytical biochemistry (01-05-1995)“…A new instrument system has been developed that automatically carries out solvent and thermal denaturations of proteins using fluorescence as a probe of…”
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11
Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins
Published in Protein engineering (01-05-2001)“…The biological activity of some proteins is known to be sensitive to oxidative damage caused by a variety of oxidants. The model protein staphylococcal…”
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12
A simplified protocol for isolation and characterization of ssM13 DNA templates for use in dideoxy sequencing
Published in BioTechniques (01-09-1993)Get more information
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13
Experimental measurement of the effective dielectric in the hydrophobic core of a protein
Published in Biophysical chemistry (28-02-1997)“…The dielectric inside a protein is a key physical determinant of the magnitude of electrostatic interactions in proteins. We have measured this dielectric…”
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14
Energetics of Side Chain Packing in Staphylococcal Nuclease Assessed by Systematic Double Mutant Cycles
Published in Biochemistry (Easton) (20-11-2001)“…All 44 possible double mutant permutations of isoleucine, leucine, and valine were constructed in 11 pairings of six sites in the core of staphylococcal…”
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15
In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core
Published in Journal of molecular biology (05-09-1991)“…The crystal structure of the staphylococcal nuclease mutant V66K, in which valine 66 is replaced by lysine, has been solved at 1.97 A resolution. Unlike lysine…”
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16
Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone
Published in Proteins, structure, function, and bioinformatics (01-06-1995)“…Changes in amino acid side chains have long been recognized to alter the range and distribution of phi, psi angles found in the main chain of polypeptides…”
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17
Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease
Published in Biochemistry (Easton) (24-10-1995)“…Hydrogen bonds are a ubiquitous feature of protein structures, yet there is great uncertainty about the energetic contribution of hydrogen bonding to protein…”
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18
Stability Effects of Increasing the Hydrophobicity of Solvent-Exposed Side Chains in Staphylococcal Nuclease
Published in Biochemistry (Easton) (12-05-1998)“…A total of fifty single site surface phenylalanine substitution mutants have been made in the model protein staphylococcal nuclease. The fifty residues that…”
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19
Application of automated methods for determination of protein conformational stability
Published in Methods in enzymology (1998)“…Automation of protein stability determination saves much time and often results in better data. In our laboratory we estimate that the lack of such…”
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20
Chemically crosslinked protein dimers: Stability and denaturation effects
Published in Protein science (01-12-1995)“…Nine single substitution cysteine mutants of staphylococcal nuclease (nuclease) were preferentially crosslinked at the introduced cysteine residues using three…”
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