Yusuf Hamied Department of Chemistry

Publications

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  • Currently displaying 22921 - 22940 of 30321 publications
Author(s)
Publication title
Journal Name
Publication year
Protein Stability as a Function of Denaturant Concentration: The Thermal Stability of Barnase in the Presence of Urea
CM Johnson, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00020a026)
Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase.
JM Matthews, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00020a027)
Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein
BB Kragelund, CV Robinson, J Knudsen, CM Dobson, FM Poulsen
Biochemistry
(2002)
34
(doi: 10.1021/bi00021a037)
The Mechanism of Metal Independent Hydroxylation by Chomobacterium violaceum Phenylalanine Hydroxylase
RT Carr, S Balasubramanian, PC Hawkins, SJ Benkovic
Biochemistry
(2002)
34
(doi: 10.1021/bi00022a028)
PEPTIDE ALDEHYDE INHIBITORS OF HEPATITIS-A VIRUS 3C PROTEINASE
BA Malcolm, C Lowe, S Shechosky, RT McKay, CC Yang, VJ Shah, RJ Simon, JC Vederas, DV Santi
Biochemistry
(2002)
34
(doi: 10.1021/bi00025a024)
Relationship between Equilibrium Amide Proton Exchange Behavior and the Folding Pathway of Bamase
S Perrett, J Clarke, AM Hounslow, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00029a003)
PK(A) VALUES OF CARBOXYL GROUPS IN THE NATIVE AND DENATURED STATES OF BARNASE - THE PK(A) VALUES OF THE DENATURED STATE ARE ON AVERAGE 0.4 UNITS LOWER THAN THOSE OF MODEL COMPOUNDS
M Oliveberg, VL Arcus, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00029a018)
Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes.
LJ Smith, AE Mark, CM Dobson, WF van Gunsteren
Biochemistry
(2002)
34
(doi: 10.1021/bi00034a026)
STRUCTURAL FACTORS CONTRIBUTING TO THE HYDROPHOBIC EFFECT - THE PARTLY EXPOSED HYDROPHOBIC MINICORE IN CHYMOTRYPSIN INHIBITOR-2
DE Otzen, M Rheinnecker, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00040a016)
Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.
M Buck, H Schwalbe, CM Dobson
Biochemistry
(2002)
34
(doi: 10.1021/bi00040a038)
Movement of the Position of the Transition State in Protein Folding
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00041a047)
Nature and consequences of GroEL-protein interactions.
LS Itzhaki, DE Otzen, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00044a037)
CONVERSION OF CYTOCHROME B(562) TO C-TYPE CYTOCHROMES
PD Barker, EP Nerou, SM Freund, IM Fearnley
Biochemistry
(2002)
34
(doi: 10.1021/bi00046a027)
Folding of subtilisin BPN': characterization of a folding intermediate
J Eder, M Rheinnecker, AR Fersht
Biochemistry
(2002)
32
(doi: 10.1021/bi00052a004)
NMR Studies of the Dynamics of the Multidomain Protein Urokinase-type Plasminogen Activator
UK Nowak, X Li, AJ Teuten, RA Smith, CM Dobson
Biochemistry
(2002)
32
(doi: 10.1021/bi00052a038)
A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding
M Buck, SE Radford, CM Dobson
Biochemistry
(2002)
32
(doi: 10.1021/bi00053a036)
Engineering a novel specificity in subtilisin BPN'
M Rheinnecker, G Baker, J Eder, AR Fersht
Biochemistry
(2002)
32
(doi: 10.1021/bi00056a001)
Structure and Dynamics of the Acid-Denatured Molten Globule State of α-Lactalbumin: A Two-Dimensional NMR Study
AT Alexandrescu, PA Evans, M Pitkeathly, J Baum, CM Dobson
Biochemistry
(2002)
32
(doi: 10.1021/bi00058a003)
Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum
AG Day, P Chène, AR Fersht
Biochemistry
(2002)
32
(doi: 10.1021/bi00059a009)
Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
J Clarke, AR Fersht
Biochemistry
(2002)
32
(doi: 10.1021/bi00067a022)
Yusuf Hamied Department of Chemistry
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CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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