J.L. Schlessman - Concepedia

Concepedia

Author

J.L. Schlessman

United States Naval Academy ORCID

Also Known As

A. Heroux, B. Garcia-Moreno E., E.B. Garcia-Moreno, J. Schlessman, J.L. Schlessman, Jamie L Schlessman, Jamie L. Schlessman, Jamie Schlessman, Jamie L. Schlessman, M.J. Harms

149

Publications

2.1K

Citations

18

H-Index

18

Concepts

All Affiliations

United States Naval Academy Johns Hopkins University Rensselaer Polytechnic Institute Johns Hopkins Medicine University of Minnesota

JS

About

J.L. Schlessman is an author at United States Naval Academy specializing in biochemistry, medicine, and natural sciences.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	13	13	1.7K
2	Natural Sciences	13	13	1.7K
3	Biochemistry	13	13	1.7K
4	Molecular Biology	10	10	1.6K
5	Microbiology	2	2	179

J.L. Schlessman

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21

Publications

2.1K

Citations

18

H-Index

	Year	Citations
Structure of ADP·AIF4–-stabilized nitrogenase complex and its implications for signal transduction Hermann Schindelin, Caroline Kisker, J.L. Schlessman, Nature Signal TransductionBiochemistryReactive Nitrogen SpecieNatural SciencesEnzyme Catalysis	1997	514
Cavities determine the pressure unfolding of proteins Julien Roche, A. José, Douglas R. Norberto, Proceedings of the National Academy of Sciences Pressure UnfoldingInternal CavitiesBiochemistryProtein AssemblyProtein Folding	2012	376
Arginine residues at internal positions in a protein are always charged Michael J. Harms, J.L. Schlessman, Gloria R. Sue, Proceedings of the National Academy of Sciences Protein AssemblyMolecular BiologyProtein SynthesisProtein FoldingProtein X-ray Crystallography	2011	184
Molecular determinants of the p<i>K</i><sub>a</sub> values of Asp and Glu residues in staphylococcal nuclease Carlos A. Castañeda, Carolyn A. Fitch, Ananya Majumdar, Proteins Structure Function and Bioinformatics	2009	164
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum J.L. Schlessman, Deborah Woo, Leemor Joshua‐Tor, Journal of Molecular Biology Nitrogenase Iron ProteinsAzotobacter VinelandiiBiochemistryReactive Nitrogen SpecieProtein Folding	1998	160
The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors Michael J. Harms, Carlos A. Castañeda, J.L. Schlessman, Journal of Molecular Biology Protein ChemistryBasic Residues BuriedProtein FunctionBiochemistryProtein Assembly	2009	153
A buried lysine that titrates with a normal p<i>K<sub>a</sub></i>: Role of conformational flexibility at the protein–water interface as a determinant of p<i>K<sub>a</sub></i>values Michael J. Harms, J.L. Schlessman, Michael S. Chimenti, Protein Science Crystal StructureProtein AssemblyProtein–water InterfaceMolecular BiologyProtein Folding	2008	85
Stabilization of Internal Charges in a Protein: Water Penetration or Conformational Change? Vladimir P. Denisov, J.L. Schlessman, Bertrand García‐Moreno E., Biophysical Journal Protein ChemistryBiochemistryProtein AssemblyProtein FoldingNatural Sciences	2004	56
Structural Reorganization Triggered by Charging of Lys Residues in the Hydrophobic Interior of a Protein Michael S. Chimenti, V.S. Khangulov, A.C. Robinson, Structure Protein ChemistryBiochemistryProtein AssemblyProtein FoldingStructural Reorganization Triggered	2012	53
Electrostatic Effects in a Network of Polar and Ionizable Groups in Staphylococcal Nuclease Kelli Baran, Michael S. Chimenti, J.L. Schlessman, Journal of Molecular Biology Nucleic Acid ChemistryElectrostatic EffectsBiochemistryStaphylococcal NucleaseProtein Folding	2008	49

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