Mutations can cause large changes in the conformation of a denatured protein.
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Toward an outline of the topography of a realistic protein-folding funnelFolding Stability and Cooperativity of the Three Forms of 1–110 Residues Fragment of Staphylococcal NucleaseA minimal sequence code for switching protein structure and functionUrea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsPartially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.Principles of protein folding--a perspective from simple exact models.The effect of Glu75 of staphylococcal nuclease on enzyme activity, protein stability and protein unfolding.The methanol-induced transition and the expanded helical conformation in hen lysozyme.The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent.Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering.A method for determining transmembrane helix association and orientation in detergent micelles using small angle x-ray scatteringPressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulationStaphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy.Isolation and characterization of a mutation that alters the substrate specificity of the Escherichia coli glucose permease.Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.Surface point mutations that significantly alter the structure and stability of a protein's denatured stateUrea-induced conformational changes in cold- and heat-denatured states of a protein, Streptomyces subtilisin inhibitorSmall-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles.Random-coil behavior and the dimensions of chemically unfolded proteins.The folding of single domain proteins--have we reached a consensus?Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Motion of polymer ends in homopolymer and heteropolymer collapse.Dependence of protein stability on the structure of the denatured state: free energy calculations of I56V mutation in human lysozyme.Cytochrome unfolding pathways from computational analysis of crystal structures.Nonlocal interactions are responsible for tertiary structure formation in staphylococcal nuclease.Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured stateStructural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.Effects of excluded volume upon protein stability in covalently cross-linked proteins with variable linker lengths.Role of C-terminal region of Staphylococcal nuclease for foldability, stability, and activity.Fractal Geometry Approach to Describe Mesostructured Boehmite and Gamma-Alumina Nanorods
P2860
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P2860
Mutations can cause large changes in the conformation of a denatured protein.
description
1993 nî lūn-bûn
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1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
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1993年學術文章
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1993年學術文章
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name
Mutations can cause large changes in the conformation of a denatured protein.
@en
Mutations can cause large changes in the conformation of a denatured protein.
@nl
type
label
Mutations can cause large changes in the conformation of a denatured protein.
@en
Mutations can cause large changes in the conformation of a denatured protein.
@nl
prefLabel
Mutations can cause large changes in the conformation of a denatured protein.
@en
Mutations can cause large changes in the conformation of a denatured protein.
@nl
P2093
P356
P1433
P1476
Mutations can cause large changes in the conformation of a denatured protein.
@en
P2093
Engelman DM
Flanagan JM
Fujisawa T
P304
10359-10370
P356
10.1021/BI00090A011
P407
P577
1993-10-01T00:00:00Z